Research workbench

Gmas in complex with amppcp

Analyse Gmas in complex with amppcp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CQN
Type: protein
Length: 1,287 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Type III glutamate--ammonia ligase
EC: 6.3.1.2
UniProt: A0A369R1N0
Ligands: ACP
Pockets: 9 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Type III glutamate--ammonia ligase (EC 6.3.1.2)	protein	429	38% helix, 21% strand	A0A369R1N0

Ligands and binding sites

ACP · Phosphomethylphosphonic acid adenylate ester · ligand · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.73	0.99	18	empty
2	679	0.70	0.78	62	empty
3	442	0.69	0.80	55	ACP
4	191	0.56	0.80	40	ACP
5	158	0.52	0.79	36	empty

Interfaces

2 interfaces between chains.

B–C · 1970 Å² buried · 29 hydrogen bonds · protein-protein
A–B · 1497 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

7CQN · GmaS in complex with AMPPCP · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A369R1N0
Elsewhere: RCSB PDB 7CQN · PDBe 7CQN · UniProt A0A369R1N0

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