MolNFT v1 · #10003 · protein

Mac-1 I domain metal free

1IDN · CD11B: “Mac-1 I domain metal free”. X-ray diffraction, 1 ligand (ACE), 1 pocket (best druggability 0.29). MolNFT v1 #10003 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1IDN
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
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1, 2	CD11B	protein	189	40% helix, 20% strand	P11215

Ligands and binding sites

ACE · Acetyl group · ligand · 2 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	72	0.29	0.73	19	empty

Interfaces

1 interface between chains.

1–2 · 232 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

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

Compared structures

1IDN · Mac-1 I domain metal free · 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 1IDN · PDBe 1IDN · UniProt P11215

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