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ABL1 SH3 PTYR89/134

Analyse ABL1 SH3 PTYR89/134 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NP2
Type: protein
Length: 118 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase ABL1
EC: 2.7.10.2
UniProt: P00519

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase ABL1 (EC 2.7.10.2)	protein	57	5% helix, 51% strand	P00519
B	Tyrosine-protein kinase ABL1 (EC 2.7.10.2)	protein	61	5% helix, 49% strand	P00519

Interfaces

1 interface between chains.

A–B · 570 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

5NP2 · Abl1 SH3 pTyr89/134 · the same entry in another collection · chain A against A, TM-score 1.00
P00519 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase ABL1 (P00519) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P00519
Elsewhere: RCSB PDB 5NP2 · PDBe 5NP2 · UniProt P00519

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