MolNFT v1 · #26474 · protein

Crystal structure of biotin-(acetyl-CoA-carboxylase) ligase from pyrococcus horikoshii OT3

1WQ7 · Biotin--[acetyl-CoA-carboxylase] ligase: “Crystal structure of biotin-(acetyl-CoA-carboxylase) ligase from pyrococcus horikoshii OT3”. X-ray diffraction, 7 pockets (best druggability 0.47). MolNFT v1 #26474 on GenesisL1: 3D…

PDB: 1WQ7
Type: protein
Length: 456 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Biotin--[acetyl-CoA-carboxylase] ligase
EC: 6.3.4.15
UniProt: O57883
Pockets: 7 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	protein	229	28% helix, 34% strand	O57883
B	Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	protein	227	26% helix, 34% strand	O57883

Pockets

7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	200	0.47	0.75	31	empty
2	83	0.38	0.77	26	empty
3	104	0.38	0.75	24	empty
4	69	0.31	0.74	25	empty
5	60	0.31	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 1070 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

1WQ7 · Crystal Structure Of Biotin-(Acetyl-CoA-Carboxylase) ligase From Pyrococcus Horikoshii Ot3 · 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
Every structure of UniProt O57883
Elsewhere: RCSB PDB 1WQ7 · PDBe 1WQ7 · UniProt O57883

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