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Catalytic domain of vahc from aeromonas hydrophila

Analyse Catalytic domain of vahc from aeromonas hydrophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FML
Type: protein
Length: 558 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vsdc
UniProt: Q49TP5
Pockets: 5 · best druggability 0.72

Structure

x-ray diffraction · 3 distinct chains · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vsdc	protein	204	33% helix, 22% strand	Q49TP5
B	Vsdc	protein	196	36% helix, 26% strand	Q49TP5
C	Vsdc	protein	158	28% helix, 25% strand	Q49TP5

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1156	0.72	0.76	94	empty
2	365	0.59	0.76	49	empty
3	215	0.56	0.79	24	empty
4	56	0.39	0.81	19	empty
5	53	0.24	0.72	12	empty

Interfaces

2 interfaces between chains.

A–C · 634 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 235 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4FML · Catalytic domain of VahC from Aeromonas hydrophila · 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 Q49TP5
Elsewhere: RCSB PDB 4FML · PDBe 4FML · UniProt Q49TP5

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