MolNFT v1 · #63315 · protein

The F4 fimbrial chaperone faee does not self-cap its interactive surfaces

3F65 · Chaperone protein faee: “The F4 fimbrial chaperone faee does not self-cap its interactive surfaces”. X-ray diffraction, 1 ligand (PO4), 20 pockets (best druggability 0.78). MolNFT v1 #63315 on GenesisL1: 3D structure, binding sites…

PDB: 3F65
Type: protein
Length: 1,484 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein faee
UniProt: P25401
Ligands: PO4
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 7 distinct chains · 5% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Chaperone protein faee	protein	206	7% helix, 46% strand	P25401
B	Chaperone protein faee	protein	205	7% helix, 46% strand	P25401
D	Chaperone protein faee	protein	161	4% helix, 42% strand	P25401
E	Chaperone protein faee	protein	194	6% helix, 43% strand	P25401
F	Chaperone protein faee	protein	166	5% helix, 43% strand	P25401
G	Chaperone protein faee	protein	193	2% helix, 46% strand	P25401
H	Chaperone protein faee	protein	153	4% helix, 43% strand	P25401

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, C, G

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	904	0.78	0.81	95	empty
2	1062	0.78	0.80	94	empty
3	955	0.78	0.80	94	empty
4	639	0.70	0.78	64	empty
5	949	0.69	0.74	84	empty

Interfaces

13 interfaces between chains.

A–D · 728 Å² buried · 15 hydrogen bonds · protein-protein
E–H · 715 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 636 Å² buried · 16 hydrogen bonds · protein-protein
E–F · 614 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 600 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

3F65 · The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces · the same entry in another collection · chain H against H, TM-score 1.00
P25401 · AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401) · a predicted model of the same protein · chain E 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 3F65 · PDBe 3F65 · UniProt P25401

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