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CAF1M periplasmic chaperone tetramer

Analyse CAF1M periplasmic chaperone tetramer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OS7
Type: protein
Length: 1,194 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein CAF1M
UniProt: P26926
Pockets: 13 · best druggability 0.83

Structure

x-ray diffraction · 6 distinct chains · 4% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein CAF1M	protein	206	5% helix, 49% strand	P26926
B	Chaperone protein CAF1M	protein	196	4% helix, 51% strand	P26926
C	Chaperone protein CAF1M	protein	205	5% helix, 53% strand	P26926
D	Chaperone protein CAF1M	protein	195	3% helix, 53% strand	P26926
E	Chaperone protein CAF1M	protein	202	5% helix, 53% strand	P26926
F	Chaperone protein CAF1M	protein	190	3% helix, 55% strand	P26926

Pockets

13 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	1150	0.83	0.84	108	empty
2	987	0.82	0.83	79	empty
3	913	0.75	0.78	70	empty
4	857	0.73	0.78	79	empty
5	136	0.65	0.88	27	empty

Interfaces

10 interfaces between chains.

A–B · 2539 Å² buried · 45 hydrogen bonds · protein-protein
E–F · 2506 Å² buried · 43 hydrogen bonds · protein-protein
C–D · 2491 Å² buried · 42 hydrogen bonds · protein-protein
D–E · 1387 Å² buried · 27 hydrogen bonds · protein-protein
C–F · 1348 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

2OS7 · Caf1M periplasmic chaperone tetramer · the same entry in another collection · chain F against F, TM-score 1.00
P26926 · AlphaFold monomer V2.0 prediction for chaperone protein CAF1M (P26926) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P26926
Elsewhere: RCSB PDB 2OS7 · PDBe 2OS7 · UniProt P26926

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