MolNFT v1 · #129628 · protein

Crystal structure of the groel mutant A109C

5OPW · 60 kda chaperonin: “Crystal structure of the groel mutant A109C”. X-ray diffraction, 20 pockets (best druggability 0.81). MolNFT v1 #129628 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5OPW
Type: protein
Length: 7,336 residues
Chains: 14
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 60 kda chaperonin
UniProt: P0A6F5
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	60 kda chaperonin	protein	524	52% helix, 19% strand	P0A6F5

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1049	0.81	0.83	100	empty
2	978	0.81	0.83	93	empty
3	987	0.81	0.83	98	empty
4	985	0.81	0.82	100	empty
5	897	0.81	0.83	86	empty

Interfaces

28 interfaces between chains.

M–N · 1833 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1780 Å² buried · 20 hydrogen bonds · protein-protein
D–E · 1779 Å² buried · 18 hydrogen bonds · protein-protein
J–K · 1765 Å² buried · 17 hydrogen bonds · protein-protein
H–I · 1748 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

5OPW · Crystal structure of the GroEL mutant A109C · the same entry in another collection · chain I against I, 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 P0A6F5
Elsewhere: RCSB PDB 5OPW · PDBe 5OPW · UniProt P0A6F5

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