Research workbench

Crystal structure of biotin carboxylase domain of acetyl- coenzyme a carboxylase from saccharomyces cerevisiae

Analyse Crystal structure of biotin carboxylase domain of acetyl- coenzyme a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W93
Type: protein
Length: 549 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-coenzyme a carboxylase
EC: 6.4.1.2
UniProt: Q00955
Pockets: 7 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-coenzyme a carboxylase (EC 6.4.1.2)	protein	549	29% helix, 17% strand	Q00955

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	431	0.65	0.78	39	empty
2	296	0.60	0.78	44	empty
3	356	0.59	0.76	46	empty
4	192	0.51	0.77	35	empty
5	171	0.47	0.76	26	empty

Compared structures

1W93 · Crystal Structure of Biotin Carboxylase Domain of Acetyl-Coenzyme A Carboxylase from… · the same entry in another collection · chain A against A, TM-score 1.00
Q00955 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase (Q00955) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q00955
Elsewhere: RCSB PDB 1W93 · PDBe 1W93 · UniProt Q00955

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