Structure of PDB 1i6o Chain A

Receptor sequence
>1i6oA (length=213) Species: 562 (Escherichia coli) [Search protein sequence]
DIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERL
TGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEVEHIIICGHYGCG
GVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVM
EQVYNLGHSTIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLE
QRYRHGISNLKLK
3D structure
PDB1i6o Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C42 D44 R46 H98 C101
Catalytic site (residue number reindexed from 1) C40 D42 R44 H96 C99
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 C40 D42 H96 C99
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1i6o, PDBe:1i6o, PDBj:1i6o
PDBsum1i6o
PubMed11316870
UniProtP61517|CAN_ECOLI Carbonic anhydrase 2 (Gene Name=can)

[Back to BioLiP]