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Crystal structure of bt-CD domains of human acetyl-CoA carboxylase

Analyse Crystal structure of bt-CD domains of human acetyl-CoA carboxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I87
Type: protein
Length: 1,385 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bt-CD domains of human acetyl-CoA carboxylase
EC: 6.4.1.2
Ligands: CD
Pockets: 14 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bt-CD domains of human acetyl-CoA carboxylase (EC 6.4.1.2)	protein	723	46% helix, 20% strand	—
B	Bt-CD domains of human acetyl-CoA carboxylase (EC 6.4.1.2)	protein	662	51% helix, 18% strand	—

Ligands and binding sites

CD · Cadmium ion · metal · 5 copies · chains A, B

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

Pockets

14 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1065	0.79	0.81	134	empty
2	983	0.76	0.79	130	empty
3	1055	0.76	0.78	146	empty
4	463	0.75	0.84	73	empty
5	923	0.74	0.78	102	empty

Interfaces

1 interface between chains.

A–B · 265 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5I87 · Crystal structure of BT-CD domains of human acetyl-CoA carboxylase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 5I87 · PDBe 5I87

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