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Structure of the PHE2 and PHE3 fragments of the integrin BETA2 subunit

Analyse Structure of the PHE2 and PHE3 fragments of the integrin BETA2 subunit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P26
Type: protein
Length: 280 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Integrin beta-2
UniProt: P05107
Ligands: NAG
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Integrin beta-2	protein	280	11% helix, 35% strand	P05107

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	236	0.50	0.75	37	empty

Modifications

Observed in the structure: 13 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

2P26 · Structure of the PHE2 and PHE3 fragments of the integrin beta2 subunit · the same entry in another collection · chain A against A, TM-score 1.00
P05107 · AlphaFold monomer V2.0 prediction for integrin beta-2 (P05107) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 P05107
Elsewhere: RCSB PDB 2P26 · PDBe 2P26 · UniProt P05107

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