MolNFT v1 · #68464 · protein

Complex of fimc, fimf, fimg and fimh

3JWN · Chaperone protein fimc: “Complex of fimc, fimf, fimg and fimh”. X-ray diffraction, 15 pockets (best druggability 0.65). MolNFT v1 #68464 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3JWN
Type: protein
Length: 1,859 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein fimc; Protein fimf; Protein fimg; Fimh protein
UniProt: P31697, P08189, P08190, Q0T8Y8
Pockets: 15 · best druggability 0.65

Structure

x-ray diffraction · 5 distinct chains · 2% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Chaperone protein fimc	protein	199	3% helix, 55% strand	P31697
E, F, K, L	Protein fimf	protein	154	3% helix, 45% strand	P08189
G, M	Protein fimg	protein	144	0% helix, 53% strand	P08190
H, N	Fimh protein	protein	279	2% helix, 52% strand	Q0T8Y8
I	Chaperone protein fimc	protein	198	3% helix, 56% strand	P31697

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains H, N

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

Pockets

15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	437	0.65	0.78	60	empty
2	330	0.61	0.78	49	empty
3	176	0.57	0.81	37	empty
4	133	0.56	0.83	26	empty
5	125	0.43	0.77	23	GOL

Interfaces

11 interfaces between chains.

I–K · 1678 Å² buried · 34 hydrogen bonds · protein-protein
C–E · 1657 Å² buried · 34 hydrogen bonds · protein-protein
G–H · 1331 Å² buried · 31 hydrogen bonds · protein-protein
M–N · 1323 Å² buried · 28 hydrogen bonds · protein-protein
L–M · 1300 Å² buried · 35 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

3JWN · Complex of FimC, FimF, FimG and FimH · the same entry in another collection · chain N against N, TM-score 1.00
P31697 · AlphaFold monomer V2.0 prediction for chaperone protein fimc (P31697) · a predicted model of the same protein · chain I against A, TM-score 0.99

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 P31697
Every structure of UniProt P08189
Every structure of UniProt P08190
Every structure of UniProt Q0T8Y8
Elsewhere: RCSB PDB 3JWN · PDBe 3JWN · UniProt P31697 · UniProt P08189 · UniProt P08190 · UniProt Q0T8Y8

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