MolNFT v1 · #78997 · protein

Structure of the major type 1 pilus subunit fima bound to the fimc chaperone

3SQB · Chaperone protein fimc: “Structure of the major type 1 pilus subunit fima bound to the fimc chaperone”. X-ray diffraction, 16 pockets (best druggability 0.71). MolNFT v1 #78997 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 3SQB
Type: protein
Length: 1,100 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein fimc; Type-1 fimbrial protein, a chain
UniProt: P31697, P04128
Pockets: 16 · best druggability 0.71

Structure

x-ray diffraction · 7 distinct chains · 4% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein fimc	protein	191	3% helix, 52% strand	P31697
B, D	Type-1 fimbrial protein, a chain	protein	145	8% helix, 46% strand	P04128
C	Chaperone protein fimc	protein	200	3% helix, 54% strand	P31697
E	Chaperone protein fimc	protein	176	3% helix, 45% strand	P31697
F	Type-1 fimbrial protein, a chain	protein	89	7% helix, 43% strand	P04128
G	Chaperone protein fimc	protein	76	0% helix, 64% strand	P31697
H	Type-1 fimbrial protein, a chain	protein	78	0% helix, 38% strand	P04128

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, B
EDO · 1,2-ethanediol · additive · 2 copies · chains C, D
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains C, D

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

Pockets

16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	567	0.71	0.80	88	empty
2	360	0.69	0.82	42	empty
3	137	0.68	0.89	36	empty
4	64	0.67	0.94	22	empty
5	534	0.61	0.74	47	empty

Interfaces

8 interfaces between chains.

A–B · 1796 Å² buried · 38 hydrogen bonds · protein-protein
C–D · 1718 Å² buried · 37 hydrogen bonds · protein-protein
E–F · 1339 Å² buried · 28 hydrogen bonds · protein-protein
G–H · 696 Å² buried · 15 hydrogen bonds · protein-protein
A–D · 473 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3SQB · Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone · the same entry in another collection · chain H against H, TM-score 1.00
P31697 · AlphaFold monomer V2.0 prediction for chaperone protein fimc (P31697) · a predicted model of the same protein · chain A 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 P04128
Elsewhere: RCSB PDB 3SQB · PDBe 3SQB · UniProt P31697 · UniProt P04128

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