MolNFT v1 · #136674 · protein

Crystal structure of C-as lyase with mutation K105A and substrate roxarsone

5V0F · GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE: “Crystal structure of C-as lyase with mutation K105A and substrate roxarsone”. X-ray diffraction, 3 ligands (RXO, FE, CL), 1 pocket (best druggability 0.48). MolNFT v1 #136674 on…

PDB: 5V0F
Type: protein
Length: 119 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE
UniProt: D1A230
Ligands: RXO, FE, CL
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE	protein	119	21% helix, 38% strand	D1A230

Ligands and binding sites

RXO · 4-arsanyl-2-nitrophenol · ligand · chains A
FE · Fe (III) ion · metal · chains A
CL · Chloride ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.48	0.83	22	RXO, FE

Compared structures

5V0F · Crystal structure of C-As lyase with mutation K105A and substrate Roxarsone · 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 D1A230
Elsewhere: RCSB PDB 5V0F · PDBe 5V0F · UniProt D1A230

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