MolNFT v1 · #187868 · protein

Structure of a bacterial fimbrial tip containing foch

7SZO · Chaperone protein fimc: “Structure of a bacterial fimbrial tip containing foch”. X-ray diffraction, 17 pockets (best druggability 0.63). MolNFT v1 #187868 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7SZO
Type: protein
Length: 1,858 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein fimc; Fimf protein; Fimg; FIMH,F1C putative fimbrial adhesin fusion
UniProt: P31697, A0A1M0WRP3, A8HPB0, Q9F6Z7, A8KI79
Pockets: 17 · best druggability 0.63

Structure

x-ray diffraction · 4 distinct chains · 2% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, I	Chaperone protein fimc	protein	198	3% helix, 55% strand	P31697
E, F, K, L	Fimf protein	protein	154	2% helix, 44% strand	A0A1M0WRP3
G, M	Fimg	protein	144	2% helix, 54% strand	A8HPB0
H, N	FIMH,F1C putative fimbrial adhesin fusion	protein	279	2% helix, 52% strand	Q9F6Z7, A8KI79

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

17 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	370	0.63	0.79	55	empty
2	140	0.58	0.84	29	empty
3	144	0.57	0.83	28	empty
4	266	0.56	0.77	38	empty
5	78	0.46	0.81	18	empty

Interfaces

11 interfaces between chains.

C–E · 1690 Å² buried · 27 hydrogen bonds · protein-protein
I–K · 1687 Å² buried · 35 hydrogen bonds · protein-protein
G–H · 1323 Å² buried · 32 hydrogen bonds · protein-protein
M–N · 1315 Å² buried · 31 hydrogen bonds · protein-protein
L–M · 1292 Å² buried · 34 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

7SZO · Structure of a bacterial fimbrial tip containing FocH · 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 A0A1M0WRP3
Every structure of UniProt A8HPB0
Every structure of UniProt Q9F6Z7
Every structure of UniProt A8KI79
Elsewhere: RCSB PDB 7SZO · PDBe 7SZO · UniProt P31697 · UniProt A0A1M0WRP3 · UniProt A8HPB0 · UniProt Q9F6Z7 · UniProt A8KI79

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