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Crystal structure of aclacinomycin-10-hydroxylase (rdmb) in complex with S-adenosyl-L-homocysteine (sah)

Analyse Crystal structure of aclacinomycin-10-hydroxylase (rdmb) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1R00
Type: protein
Length: 340 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aclacinomycin-10-hydroxylase
UniProt: Q54527
Ligands: SAH
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aclacinomycin-10-hydroxylase	protein	340	51% helix, 16% strand	Q54527

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

2 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	889	0.79	0.81	86	ACT, SAH
2	51	0.26	0.73	11	empty

Compared structures

1R00 · Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Q54527 · AlphaFold monomer V2.0 prediction for aclacinomycin 10-hydroxylase rdmb (Q54527) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 Q54527
Elsewhere: RCSB PDB 1R00 · PDBe 1R00 · UniProt Q54527

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