MolNFT v1 · #43438 · protein

Solution structure of the VAV1 SH2 domain complexed with a syk-derived doubly phosphorylated peptide

2LCT · Proto-oncogene vav: “Solution structure of the VAV1 SH2 domain complexed with a syk-derived doubly phosphorylated peptide”. Solution nmr. MolNFT v1 #43438 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2LCT
Type: protein
Length: 120 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene vav; Tyrosine-protein kinase syk
EC: 2.7.10.2
UniProt: P15498, P48025

Structure

solution nmr · 2 distinct chains · 18% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene vav	protein	107	21% helix, 27% strand	P15498
B	Tyrosine-protein kinase syk (EC 2.7.10.2)	protein	13	0% helix, 0% strand	P48025

Interfaces

1 interface between chains.

A–B · 645 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

2LCT · Solution structure of the Vav1 SH2 domain complexed with a Syk-derived doubly… · the same entry in another collection · chain A against A, TM-score 1.00
P15498 · AlphaFold monomer V2.0 prediction for proto-oncogene vav (P15498) · a predicted model of the same protein · chain A against A, TM-score 0.84
P48025 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase syk (P48025) · a predicted model of the same protein · chain B against A, TM-score 0.30

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 P15498
Every structure of UniProt P48025
Elsewhere: RCSB PDB 2LCT · PDBe 2LCT · UniProt P15498 · UniProt P48025

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