OCA Atlas for 1HTQ

1HTQ

Ligase

date

Jan 01, 2001

title

Multicopy Crystallographic Structure Of A Relaxed Glutamine Synthetase From Mycobacterium Tuberculosis

authors

H.S.Gill, G.M.Pfluegl, D.Eisenberg, Tb Structural Genomics Consortium (Tbsgc)

compound

source

Molecule: Glutamine Synthetase
Chain: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X;
Synonym: Gs, Glutamate--Ammonia Ligase 1
Ec: 6.3.1.2
Engineered: Yes

Organism_scientific: Mycobacterium Tuberculosis
Expression_system: Escherichia Coli
Expression_system_strain: Ymc21e
Expression_system_vector_type: Plasmid
Expression_system_plasmid: Ptrchisb

symmetry

Space Group: P 21 21 21

R_factor

0.204

crystal
cell

length a	length b	length c	angle alpha	angle beta	angle gamma
207.720	257.690	274.500	90.00	90.00	90.00

method

X-Ray Diffraction

resolution

2.40 Å

ligand

AMP, CIT, MN

enzyme

Glutamate-ammonia ligase;. Glutamine synthetase;. Glutamylhydroxamic synthetase;. L-glutamine synthetase. Ligase E.C.6.3.1.2 BRENDA

similarity

Belongs to the glutamine synthetase family.[Gln-synt_C]

subunit

Oligomer of 12 subunits arranged in the form of two hexagons (by similarity).

catalytic activ.

Atp + l-glutamate + nh(3) = adp + phosphate + l-glutamine.

subcellular loc.

Cytoplasm (by similarity).

enzyme regulation

The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive (by similarity).

gene

MTCY427.01 (M. tuberculosis); glnA (S. typhimurium)

Gene
Ontology

Chain	Function	Process	Component
F, N, K, E, Q, M, C, L, A, J, O, P, B, H, D, I, G	nucleotide binding glutamate-ammonia ligase act... ligase activity	glutamine biosynthetic proce... nitrogen compound metabolic ... nitrogen fixation	cytoplasm

Primary reference

Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation., Gill HS, Pfluegl GM, Eisenberg D, Biochemistry 2002 Aug 6;41(31):9863-72. PMID:12146952

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (20680 Kb) [Save to disk]

Biological Unit Coordinates (1htq.pdb1.gz) 8841 Kb

Biological Unit Coordinates (1htq.pdb2.gz) 931 Kb

CSU: Contacts of Structural Units for 1HTQ

Likely Quarternary Molecular Structure file(s) for 1HTQ

Structure Factors (4250 Kb)

Retrieve 1HTQ in mmCIF format [Save to disk]

View 1HTQ in 3D

On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure.

On FirstGlance, an excellent tool for a guided tour on the structure components, by E. Martz.

On AstexViewer, from MSD-EBI (viewer documentation).

On RasMol (Install RasMol freeware) Here's help on how to use RasMol.

Visual 3D analysis of 1HTQ

Protein Explorer, Easier to use and more powerful than RasMol. (Win and Mac only)

Noncovalent Bond Finder displays the closest contacts to ligand or interface, reports distances, walks over water bridges.

STING, shows the sequence and maps the locations of sequence residues or residue ranges onto the 3D structure.

GRASS (Graphical Representation and Analysis of Structure Server)

Cartoon representation from PDB Cartoon

Ramachandran plot from PDBSum

Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute

Crystal Contacts, from CryCo at Weizmann Institute

3D motif for 1HTQ, from MSDmotif at EBI

Classification of representative domains in scop (Structural Classification of Proteins)
- Domain d1htqa1, region A:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqa2, region A:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqb1, region B:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqb2, region B:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqc1, region C:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqc2, region C:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqd1, region D:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqd2, region D:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqe1, region E:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqe2, region E:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqf1, region F:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqf2, region F:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqg1, region G:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqg2, region G:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqh1, region H:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqh2, region H:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqi1, region I:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqi2, region I:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqj1, region J:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqj2, region J:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqk1, region K:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqk2, region K:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htql1, region L:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htql2, region L:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqm1, region M:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqm2, region M:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqn1, region N:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqn2, region N:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqo1, region O:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqo2, region O:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqp1, region P:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqp2, region P:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqq1, region Q:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqq2, region Q:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqr1, region R:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqr2, region R:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqs1, region S:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqs2, region S:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqt1, region T:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqt2, region T:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqu1, region U:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqu2, region U:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqv1, region V:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqv2, region V:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqw1, region W:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqw2, region W:101-468 [Jmol] [rasmolscript] [script source]
- Domain d1htqx1, region X:1-100 [Jmol] [rasmolscript] [script source]
- Domain d1htqx2, region X:101-468 [Jmol] [rasmolscript] [script source]

Fold representative 1htq from FSSP and Dali (Families of Structurally Similar Proteins)

Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH

Summaries and structural analyses of PDB data files from PDBSum

Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1htq_L] [1htq_Q] [1htq_U] [1htq_G] [1htq_T] [1htq_O] [1htq_C] [1htq_F] [1htq_X] [1htq_K] [1htq_P] [1htq_N] [1htq_E] [1htq_W] [1htq_H] [1htq_R] [1htq_S] [1htq_I] [1htq_M] [1htq_V] [1htq_A] [1htq_B] [1htq_J] [1htq_D]

Other resources with information on 1HTQ

InterPro: IPR004809 , IPR008146 , IPR008147 , IPR001637

MMDB (Entrez's Structure Database)

Movements, Movies and Images

Images from IMB Jena Image Library of Biological Macromolecules.

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