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Solution NMR structure of homodimer VP2129 from vibrio parahaemolyticus. northeast structural genomics consortium target VPR61.

Analyse Solution NMR structure of homodimer VP2129 from vibrio parahaemolyticus.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JPQ
Type: protein
Length: 166 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: UPF0352 protein VP2129
UniProt: Q87MV2
Pockets: 3 · best druggability 0.51

Structure

solution nmr · 1 distinct chain · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	UPF0352 protein VP2129	protein	83	65% helix, 0% strand	Q87MV2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	144	0.51	0.79	21	empty
2	113	0.48	0.79	21	empty
3	62	0.37	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 2455 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

2JPQ · Solution NMR structure of homodimer VP2129 from Vibrio parahaemolyticus. Northeast… · the same entry in another collection · chain A against A, TM-score 1.00
Q87MV2 · AlphaFold monomer V2.0 prediction for UPF0352 protein VP2129 (Q87MV2) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 Q87MV2
Elsewhere: RCSB PDB 2JPQ · PDBe 2JPQ · UniProt Q87MV2

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