Research workbench

Crystal structure of biotin protein ligase from pyrococcus horikoshii, mutations R48A and K111A

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

PDB: 2E64
Type: protein
Length: 461 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: 5 · best druggability 0.61

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	protein	226	27% helix, 31% strand	O57883
B	Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)	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	256	0.61	0.80	40	empty
2	145	0.47	0.77	26	empty
3	104	0.43	0.77	19	empty
4	158	0.40	0.73	31	empty
5	69	0.31	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 1067 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

2E64 · Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii, Mutations R48A and… · 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 2E64 · PDBe 2E64 · UniProt O57883

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.