MolNFT v1 · #26497 · protein

Crystal structure of biotin protein ligase from pyrococcus horikoshii OT3 in complex with biotinyl-5-AMP

1WQW · Biotin--[acetyl-CoA-carboxylase] ligase: “Crystal structure of biotin protein ligase from pyrococcus horikoshii OT3 in complex with biotinyl-5-AMP”. X-ray diffraction, 1 ligand (BT5), 4 pockets (best druggability 0.65). MolNFT v1…

PDB: 1WQW
Type: protein
Length: 470 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
Ligands: BT5
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	protein	235	26% helix, 33% strand	O57883

Ligands and binding sites

BT5 · Biotinyl-5-amp · ligand · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	348	0.65	0.80	45	BT5
2	225	0.62	0.82	40	BT5
3	119	0.46	0.78	20	empty
4	100	0.42	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 1032 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

1WQW · Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3 in complex with… · 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 1WQW · PDBe 1WQW · UniProt O57883

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