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PDBsum entry 1crm

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protein ligands metals links
Lyase (oxo-acid) PDB id
1crm
Jmol
Contents
Protein chain
256 a.a. *
Ligands
H2S
Metals
_HG ×4
_CL ×2
Waters ×262
* Residue conservation analysis
PDB id:
1crm
Name: Lyase (oxo-acid)
Title: Structure and function of carbonic anhydrases
Structure: Carbonic anhydrase i. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Resolution:
2.00Å     R-factor:   0.177    
Authors: V.S.Yadava,K.K.Kannan
Key ref: K.K.Kannan (1981). Structure and function of carbonic anhydrases. Biomolecular structure, Conformation, Function and evolution, 1, 165.
Date:
04-Mar-94     Release date:   07-Feb-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00915  (CAH1_HUMAN) -  Carbonic anhydrase 1
Seq:
Struc:
261 a.a.
256 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.1  - Carbonate dehydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: H2CO3 = CO2 + H2O
H(2)CO(3)
= CO(2)
+ H(2)O
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   3 terms 
  Biological process     small molecule metabolic process   3 terms 
  Biochemical function     lyase activity     4 terms