Research workbench

Faee-faeg chaperone-major pilin complex of F4 ac 5/95 fimbriae

Analyse Faee-faeg chaperone-major pilin complex of F4 ac 5/95 fimbriae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GFU
Type: protein
Length: 860 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein faee; Faeg
UniProt: P25401, Q6T3W5
Ligands: SO4
Pockets: 8 · best druggability 0.70

Structure

x-ray diffraction · 4 distinct chains · 9% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Chaperone protein faee	protein	210	7% helix, 45% strand	P25401
D	Faeg	protein	219	10% helix, 42% strand	Q6T3W5
A	Chaperone protein faee	protein	211	7% helix, 43% strand	P25401
B	Faeg	protein	220	11% helix, 41% strand	Q6T3W5

Ligands and binding sites

SO4 · Sulfate ion · ion · 11 copies · chains C, A, D, B

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

Pockets

8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	729	0.70	0.77	74	SO4
2	240	0.70	0.86	37	empty
3	717	0.69	0.77	69	SO4
4	152	0.68	0.88	37	empty
5	114	0.67	0.90	33	empty

Interfaces

5 interfaces between chains.

C–D · 1647 Å² buried · 24 hydrogen bonds · protein-protein
A–B · 1617 Å² buried · 24 hydrogen bonds · protein-protein
C–A · 693 Å² buried · 17 hydrogen bonds · protein-protein
C–B · 103 Å² buried · 0 hydrogen bonds · protein-protein
D–A · 97 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3GFU · FaeE-FaeG chaperone-major pilin complex of F4 ac 5/95 fimbriae · the same entry in another collection · chain C against C, TM-score 1.00
P25401 · AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401) · a predicted model of the same protein · chain C against A, TM-score 1.00

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
Every structure of UniProt Q6T3W5
Elsewhere: RCSB PDB 3GFU · PDBe 3GFU · UniProt P25401 · UniProt Q6T3W5

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