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Abl2 SH3

Analyse Abl2 SH3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NP3
Type: protein
Length: 232 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Homo sapiens
Molecule: Abelson tyrosine-protein kinase 2
EC: 2.7.10.2
UniProt: P42684
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · resolution 2 · 3 distinct chains · 5% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Abelson tyrosine-protein kinase 2 (EC 2.7.10.2)	protein	57	5% helix, 47% strand	P42684
B	Abelson tyrosine-protein kinase 2 (EC 2.7.10.2)	protein	58	5% helix, 48% strand	P42684
D	Abelson tyrosine-protein kinase 2 (EC 2.7.10.2)	protein	60	5% helix, 48% strand	P42684

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	62	0.28	0.73	14	empty

Interfaces

6 interfaces between chains.

C–D · 538 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 527 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 487 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 435 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 81 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5NP3 · ABL2 SH3 · the same entry in another collection · chain D against D, TM-score 1.00
P42684 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase ABL2 (P42684) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P42684
Elsewhere: RCSB PDB 5NP3 · PDBe 5NP3 · UniProt P42684

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