Structure of PDB 1i6p Chain A

Receptor sequence
>1i6pA (length=214) Species: 562 (Escherichia coli) [Search protein sequence]
KDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAER
LTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEVEHIIICGHYGC
GGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNV
MEQVYNLGHSTIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETL
EQRYRHGISNLKLK
3D structure
PDB1i6p Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C42 D44 R46 H98 C101
Catalytic site (residue number reindexed from 1) C41 D43 R45 H97 C100
Enzyme Commision number 4.2.1.1: carbonic anhydrase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A C42 D44 H98 C101 C41 D43 H97 C100
Gene Ontology
Molecular Function
GO:0004089 carbonate dehydratase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0015976 carbon utilization
GO:0051289 protein homotetramerization
Cellular Component
GO:0005829 cytosol

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Biological Process
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Cellular Component
External links
PDB RCSB:1i6p, PDBe:1i6p, PDBj:1i6p
PDBsum1i6p
PubMed11316870
UniProtP61517|CAN_ECOLI Carbonic anhydrase 2 (Gene Name=can)

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