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PDBsum entry 5c11

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protein ligands metals links
Hydrolase PDB id
5c11

 

 

 

 

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Contents
Protein chain
52 a.a.
Ligands
ALA-ARG-THR-4WQ-
GLN-THR-ALA
Metals
_ZN ×2
PDB id:
5c11
Name: Hydrolase
Title: Crystal structure of jarid1a phd finger bound to histone h3c4me3 peptide
Structure: Lysine-specific demethylase 5a. Chain: a. Fragment: phd finger domain, unp residues 1609-1659. Synonym: histone demethylase jarid1a,jumonji/arid domain-containing protein 1a,retinoblastoma-binding protein 2,rbbp-2. Engineered: yes. H3 peptide. Chain: b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: kdm5a, jarid1a, rbbp2, rbp2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.
Resolution:
2.80Å     R-factor:   0.248     R-free:   0.279
Authors: J.Huang,H.Li
Key ref: J.Huang and h.li Crystal structure of jarid1a phd finger bound to hist h3c4me3 peptide. Nat commun, .
Date:
12-Jun-15     Release date:   25-Nov-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P29375  (KDM5A_HUMAN) -  Lysine-specific demethylase 5A from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1690 a.a.
52 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.14.11.67  - [histone H3]-trimethyl-L-lysine(4) demethylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N6,N6,N6-trimethyl-L-lysyl4-[histone H3] + 3 2-oxoglutarate + 3 O2 = L-lysyl4-[histone H3] + 3 formaldehyde + 3 succinate + 3 CO2
N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3]
Bound ligand (Het Group name = GLN)
matches with 58.33% similarity
+ 3 × 2-oxoglutarate
+ 3 × O2
= L-lysyl(4)-[histone H3]
+
3 × formaldehyde
Bound ligand (Het Group name = ALA)
matches with 40.00% similarity
+ 3 × succinate
+
3 × CO2
Bound ligand (Het Group name = THR)
matches with 50.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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