MolNFT v1 · #120678 · protein

Biotin carboxylase domain of single-chain bacterial carboxylase

5H80: “Biotin carboxylase domain of single-chain bacterial carboxylase”. X-ray diffraction, 8 pockets (best druggability 0.82). MolNFT v1 #120678 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5H80
Type: protein
Length: 856 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxylase
UniProt: Q9RYK2
Pockets: 8 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxylase	protein	430	36% helix, 23% strand	Q9RYK2
B	Carboxylase	protein	426	38% helix, 25% strand	Q9RYK2

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 7 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1114	0.82	0.83	131	EDO
2	578	0.70	0.78	54	empty
3	534	0.67	0.77	57	empty
4	50	0.43	0.84	21	empty
5	53	0.31	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 986 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5H80 · Biotin Carboxylase domain of single-chain bacterial carboxylase · 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 Q9RYK2
Elsewhere: RCSB PDB 5H80 · PDBe 5H80 · UniProt Q9RYK2

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