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Structure of the semet labeled F4 fibrial chaperone faee

Analyse Structure of the semet labeled F4 fibrial chaperone faee in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3F6I
Type: protein
Length: 382 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein faee
UniProt: P25401
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein faee	protein	199	7% helix, 47% strand	P25401
B	Chaperone protein faee	protein	183	5% helix, 46% strand	P25401

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	125	0.55	0.82	20	empty
2	105	0.40	0.76	31	empty

Interfaces

1 interface between chains.

A–B · 628 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

3F6I · Structure of the SeMet labeled F4 fibrial chaperone FaeE · the same entry in another collection · chain A against A, TM-score 1.00
P25401 · AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P25401
Elsewhere: RCSB PDB 3F6I · PDBe 3F6I · UniProt P25401

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