MolNFT v1 · #13467 · protein

SH2 (src homology-2) domain of human P56-lck tyrosine kinase complexed with the 11 residue phosphotyrosyl peptide epqpyeeipiyl

1LCJ · P56==LCK== tyrosine kinase: “SH2 (src homology-2) domain of human P56-lck tyrosine kinase complexed with the 11 residue phosphotyrosyl…”. X-ray diffraction. MolNFT v1 #13467 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1LCJ
Type: protein
Length: 115 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P56==LCK== tyrosine kinase; Phosphopeptide EPQ(PHOSPHO)YEEIPIYL
EC: 2.7.1.112
UniProt: P06239, P03079

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P56==LCK== tyrosine kinase (EC 2.7.1.112)	protein	104	17% helix, 31% strand	P06239
B	Phosphopeptide EPQ(PHOSPHO)YEEIPIYL	protein	11	0% helix, 9% strand	P03079

Interfaces

1 interface between chains.

A–B · 502 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

1LCJ · SH2 (src homology-2) domain of human P56-lck tyrosine kinase complexed with the 11… · the same entry in another collection · chain A against A, TM-score 1.00
P06239 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase lck (P06239) · 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 P06239
Every structure of UniProt P03079
Elsewhere: RCSB PDB 1LCJ · PDBe 1LCJ · UniProt P06239 · UniProt P03079

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