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Crystal structure of human ALKBH5 in complex with citrate and acetate

Analyse Crystal structure of human ALKBH5 in complex with citrate and acetate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NRM
Type: protein
Length: 211 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA demethylase ALKBH5
EC: 1.14.11.-
UniProt: Q6P6C2
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA demethylase ALKBH5 (EC 1.14.11.-)	protein	211	28% helix, 29% strand	Q6P6C2

Ligands and binding sites

FLC · Citrate anion · additive · chains A
ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	202	0.67	0.85	33	FLC, ACT

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4NRM · Crystal structure of human ALKBH5 in complex with citrate and acetate · the same entry in another collection · chain A against A, TM-score 1.00
Q6P6C2 · AlphaFold monomer V2.0 prediction for RNA demethylase ALKBH5 (Q6P6C2) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q6P6C2
Elsewhere: RCSB PDB 4NRM · PDBe 4NRM · UniProt Q6P6C2

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