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Disulfide deficient mutant of vascular endothelial growth factor a (C51A and C60A)

Analyse Disulfide deficient mutant of vascular endothelial growth factor a (C51A and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MJV
Type: protein
Length: 192 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vascular endothelial growth factor a
UniProt: P15692
Pockets: 2 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 60% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Vascular endothelial growth factor a	protein	96	13% helix, 60% strand	P15692

Pockets

2 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	91	0.33	0.73	20	empty
2	61	0.30	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 1227 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1MJV · DISULFIDE DEFICIENT MUTANT OF VASCULAR ENDOTHELIAL GROWTH FACTOR A (C51A and C60A) · the same entry in another collection · chain A against A, TM-score 1.00
P15692 · AlphaFold monomer V2.0 prediction for vascular endothelial growth factor a (P15692) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P15692
Elsewhere: RCSB PDB 1MJV · PDBe 1MJV · UniProt P15692

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