MolNFT v1 · #108685 · protein

Co-complex structure of the F4 fimbrial adhesin faeg variant ac with llama single domain antibody V2

4WEN · K88 fimbrial protein ac: “Co-complex structure of the F4 fimbrial adhesin faeg variant ac with llama single domain antibody V2”. X-ray diffraction, 3 pockets (best druggability 0.50). MolNFT v1 #108685 on GenesisL1: 3D structure…

PDB: 4WEN
Type: protein
Length: 374 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: K88 fimbrial protein ac; Anti-F4+ETEC bacteria vhh variable region
UniProt: L7XD53, R9VYW2
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	K88 fimbrial protein ac	protein	253	9% helix, 45% strand	L7XD53
B	Anti-F4+ETEC bacteria vhh variable region	protein	121	5% helix, 48% strand	R9VYW2

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	192	0.50	0.76	22	empty
2	64	0.45	0.83	21	empty
3	90	0.35	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 701 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4WEN · Co-complex structure of the F4 fimbrial adhesin FaeG variant ac with llama single domain… · the same entry in another collection · chain A 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 L7XD53
Every structure of UniProt R9VYW2
Elsewhere: RCSB PDB 4WEN · PDBe 4WEN · UniProt L7XD53 · UniProt R9VYW2

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