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Crystal structure of biotin protein ligase from pyrococcus horikoshii, mutation R51A

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

PDB: 2E10
Type: protein
Length: 439 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Biotin protein ligase
EC: 6.3.4.15
UniProt: O57883
Pockets: 5 · best druggability 0.44

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biotin protein ligase (EC 6.3.4.15)	protein	217	26% helix, 32% strand	O57883
B	Biotin protein ligase (EC 6.3.4.15)	protein	222	28% helix, 31% strand	O57883

Pockets

5 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	168	0.44	0.75	30	empty
2	102	0.43	0.77	18	empty
3	109	0.36	0.74	25	empty
4	88	0.35	0.74	17	empty
5	74	0.31	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 1070 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

2E10 · Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii, Mutation R51A · 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 2E10 · PDBe 2E10 · UniProt O57883

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