MolNFT v1 · #44670 · protein

NMR spatial structure of the trimeric mutant tm domain of VEGFR2 receptor.

2MET · Vascular endothelial growth factor receptor 2: “NMR spatial structure of the trimeric mutant tm domain of VEGFR2 receptor.”. Solution nmr, 1 pocket (best druggability 0.43). MolNFT v1 #44670 on GenesisL1: 3D structure, binding sites…

PDB: 2MET
Type: protein
Length: 111 residues
Chains: 3
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vascular endothelial growth factor receptor 2
EC: 2.7.10.1
UniProt: P35968
Pockets: 1 · best druggability 0.43

Structure

solution nmr · 1 distinct chain · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Vascular endothelial growth factor receptor 2 (EC 2.7.10.1)	protein	37	81% helix, 0% strand	P35968

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	129	0.43	0.75	16	empty

Interfaces

3 interfaces between chains.

B–C · 342 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 339 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 336 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2MET · NMR spatial structure of the trimeric mutant TM domain of VEGFR2 receptor. · the same entry in another collection · chain C against C, TM-score 1.00
P35968 · AlphaFold monomer V2.0 prediction for vascular endothelial growth factor receptor 2… · a predicted model of the same protein · chain A against A, TM-score 0.56

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 P35968
Elsewhere: RCSB PDB 2MET · PDBe 2MET · UniProt P35968

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