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Src-derived mutant peptide inhibitor complex of PTP1B

Analyse Src-derived mutant peptide inhibitor complex of PTP1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZMQ
Type: protein
Length: 264 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein phosphatase non-receptor type 1; Proto-oncogene tyrosine-protein kinase…
EC: 3.1.3.48, 2.7.10.2
UniProt: P18031, P12931
Pockets: 2 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48)	protein	258	31% helix, 22% strand	P18031
C	Proto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)	protein	6	0% helix, 0% strand	P12931

Pockets

2 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	65	0.31	0.74	18	empty
2	54	0.26	0.73	13	empty

Interfaces

1 interface between chains.

A–C · 527 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

3ZMQ · Src-derived mutant peptide inhibitor complex of PTP1B · 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 P18031
Every structure of UniProt P12931
Elsewhere: RCSB PDB 3ZMQ · PDBe 3ZMQ · UniProt P18031 · UniProt P12931

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