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CD11A I-domain with bound magnesium ion

Analyse CD11A I-domain with bound magnesium ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZOO
Type: protein
Length: 366 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Leukocyte adhesion glycoprotein
UniProt: P20701
Ligands: MG, CL
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Leukocyte adhesion glycoprotein	protein	183	39% helix, 25% strand	P20701

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	250	0.69	0.84	25	empty
2	216	0.67	0.84	24	empty

Interfaces

1 interface between chains.

A–B · 1133 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

1ZOO · CD11A I-domain with bound magnesium ion · the same entry in another collection · chain A against A, TM-score 1.00
P20701 · AlphaFold monomer V2.0 prediction for integrin alpha-L (P20701) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P20701
Elsewhere: RCSB PDB 1ZOO · PDBe 1ZOO · UniProt P20701

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