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Crystal structure of the VP0956 protein from vibrio parahaemolyticus. northeast structural genomics consortium target VPR147

Analyse Crystal structure of the VP0956 protein from vibrio parahaemolyticus. northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NLC
Type: protein
Length: 534 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein VP0956
UniProt: Q87R42
Ligands: FAD
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein VP0956	protein	534	31% helix, 24% strand	Q87R42

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	291	0.83	0.94	55	FAD
2	562	0.69	0.78	65	empty
3	64	0.31	0.75	14	empty

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

3NLC · Crystal structure of the VP0956 protein from Vibrio parahaemolyticus. Northeast… · 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 Q87R42
Elsewhere: RCSB PDB 3NLC · PDBe 3NLC · UniProt Q87R42

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