MolNFT v2 · #152752 · protein

Structure of the citryl-CoA lyase core module of human ATP citrate lyase in complex with citrate

6HXK: “Structure of the citryl-CoA lyase core module of human ATP citrate lyase in complex with citrate”. X-ray diffraction at 1.85. MolNFT v2 #152752 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HXK
Type: protein
Length: 1,043 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.85
Source: Homo sapiens
UniProt: P53396

Structure

x-ray diffraction · resolution 1.85 · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	262	—	P53396
B	—	protein	261	—	P53396
C, D	—	protein	260	—	P53396

Ligands and binding sites

FLC · Citrate anion · additive · 4 copies · chains A, C, B, D
EDO · 1,2-ethanediol · additive · 3 copies · chains A, D
PGE · Triethylene glycol · additive · 2 copies · chains A, B, C, D
1PE · Pentaethylene glycol · additive · chains C, D
PEG · Di(hydroxyethyl)ether · additive · chains C

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

Compared structures

6HXK · Structure of the citryl-CoA lyase core module of human ATP citrate lyase in complex with… · the same entry in another collection · chain D against D, TM-score 1.00
P53396 · AlphaFold monomer V2.0 prediction for ATP-citrate synthase (P53396) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 P53396
Elsewhere: RCSB PDB 6HXK · PDBe 6HXK · UniProt P53396

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