Research workbench

Mac-1 I domain cadmium complex

Analyse Mac-1 I domain cadmium complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BHQ
Type: protein
Length: 378 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CD11B
UniProt: P11215
Ligands: ACE, CD
Pockets: 1 · best druggability 0.25

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1, 2	CD11B	protein	189	38% helix, 20% strand	P11215

Ligands and binding sites

ACE · Acetyl group · ligand · 2 copies · chains 1, 2
CD · Cadmium ion · metal · 3 copies · chains 1, 2

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	50	0.25	0.73	14	empty

Interfaces

1 interface between chains.

1–2 · 247 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

1BHQ · Mac-1 I domain cadmium complex · the same entry in another collection · chain 1 against 1, TM-score 1.00
P11215 · AlphaFold monomer V2.0 prediction for integrin alpha-M (P11215) · a predicted model of the same protein · chain 1 against A, TM-score 0.99

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 P11215
Elsewhere: RCSB PDB 1BHQ · PDBe 1BHQ · UniProt P11215

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