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Cmli (chemically reduced state), arylamine oxygenase of chloramphenicol biosynthetic pathway

Analyse Cmli (chemically reduced state), arylamine oxygenase of chloramphenicol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HYH
Type: protein
Length: 287 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: F2RB83
Ligands: FE
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	287	75% helix, 0% strand	F2RB83

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A
TLA · L(+)-tartaric acid · additive · chains A

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

Pockets

3 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	127	0.67	0.89	28	empty
2	60	0.36	0.78	13	empty
3	64	0.31	0.75	19	TLA

Compared structures

5HYH · CmlI (chemically reduced state), arylamine oxygenase of chloramphenicol biosynthetic… · the same entry in another collection · chain A against A, TM-score 1.00
F2RB83 · AlphaFold monomer V2.0 prediction for non-heme di-iron N-oxygenase (F2RB83) · a predicted model of the same protein · 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 F2RB83
Elsewhere: RCSB PDB 5HYH · PDBe 5HYH · UniProt F2RB83

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