9EBZ

Escherichia coli Carbonic Anhydrase 2 in Space Group C222(1)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0015976	biological_process	carbon utilization
A	0016829	molecular_function	lyase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
B	0004089	molecular_function	carbonate dehydratase activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0008270	molecular_function	zinc ion binding
B	0015976	biological_process	carbon utilization
B	0016829	molecular_function	lyase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
C	0004089	molecular_function	carbonate dehydratase activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0008270	molecular_function	zinc ion binding
C	0015976	biological_process	carbon utilization
C	0016829	molecular_function	lyase activity
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0051289	biological_process	protein homotetramerization
D	0004089	molecular_function	carbonate dehydratase activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0008270	molecular_function	zinc ion binding
D	0015976	biological_process	carbon utilization
D	0016829	molecular_function	lyase activity
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0051289	biological_process	protein homotetramerization

Functional Information from PROSITE/UniProt

site_id	PS00704
Number of Residues	8
Details	PROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CSDSRVpA

Chain	Residue	Details
A	CYS42-ALA49

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site_id	PS00705
Number of Residues	21
Details	PROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QYAVdvLevehIIIcGHygCG

Chain	Residue	Details
A	GLN82-GLY102

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11316870","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I6O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1I6P","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 517

Chain	Residue	Details
A	CYS42	metal ligand
A	ASP44	metal ligand, proton acceptor
A	ARG46	electrostatic stabiliser, increase basicity
A	HIS98	metal ligand
A	CYS101	metal ligand

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 517

Chain	Residue	Details
B	CYS42	metal ligand
B	ASP44	metal ligand, proton acceptor
B	ARG46	electrostatic stabiliser, increase basicity
B	HIS98	metal ligand
B	CYS101	metal ligand

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site_id	MCSA3
Number of Residues	5
Details	M-CSA 517

Chain	Residue	Details
C	CYS42	metal ligand
C	ASP44	metal ligand, proton acceptor
C	ARG46	electrostatic stabiliser, increase basicity
C	HIS98	metal ligand
C	CYS101	metal ligand

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site_id	MCSA4
Number of Residues	5
Details	M-CSA 517

Chain	Residue	Details
D	CYS42	metal ligand
D	ASP44	metal ligand, proton acceptor
D	ARG46	electrostatic stabiliser, increase basicity
D	HIS98	metal ligand
D	CYS101	metal ligand

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