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Crystal structure of biotin protein ligase from aquifex aeolicus

Analyse Crystal structure of biotin protein ligase from aquifex aeolicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EAY
Type: protein
Length: 441 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: O66837
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biotin [acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	protein	219	28% helix, 36% strand	O66837
B	Biotin [acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	protein	222	27% helix, 35% strand	O66837

Pockets

3 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	240	0.48	0.74	30	empty
2	102	0.44	0.78	16	empty
3	115	0.36	0.73	21	empty

Interfaces

1 interface between chains.

A–B · 561 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2EAY · Crystal Structure Of Biotin Protein Ligase From Aquifex Aeolicus · 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 O66837
Elsewhere: RCSB PDB 2EAY · PDBe 2EAY · UniProt O66837

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