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Crystal structure of biotin protein ligase from pyrococcus horikoshii OT3, K111G mutation

Analyse Crystal structure of biotin protein ligase from pyrococcus horikoshii OT3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2E1H
Type: protein
Length: 460 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 235AA long hypothetical biotin-[acetyl-CoA-carboxylase] ligase
UniProt: O57883
Pockets: 5 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	235AA long hypothetical biotin-[acetyl-CoA-carboxylase] ligase	protein	225	28% helix, 31% strand	O57883
B	235AA long hypothetical biotin-[acetyl-CoA-carboxylase] ligase	protein	235	27% helix, 31% strand	O57883

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	228	0.55	0.78	32	empty
2	211	0.49	0.76	39	empty
3	123	0.46	0.77	23	empty
4	106	0.44	0.77	18	empty
5	64	0.36	0.78	15	empty

Interfaces

1 interface between chains.

A–B · 1013 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

2E1H · Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii OT3, K111G mutation · 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 2E1H · PDBe 2E1H · UniProt O57883

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