Research workbench

Vegfr-2/VEGF-E complex structure

Analyse Vegfr-2/VEGF-E complex structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3V6B
Type: protein
Length: 281 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VEGF-E; Vascular endothelial growth factor receptor 2
EC: 2.7.10.1
UniProt: Q2F842, P35968
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VEGF-E	protein	94	13% helix, 62% strand	Q2F842
R	Vascular endothelial growth factor receptor 2 (EC 2.7.10.1)	protein	187	3% helix, 54% strand	P35968

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	112	0.46	0.79	17	empty
2	61	0.33	0.77	17	empty
3	51	0.25	0.73	11	empty

Interfaces

1 interface between chains.

A–R · 640 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

3V6B · VEGFR-2/VEGF-E complex structure · 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 Q2F842
Every structure of UniProt P35968
Elsewhere: RCSB PDB 3V6B · PDBe 3V6B · UniProt Q2F842 · UniProt P35968

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