4CNR

Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0008270	molecular_function	zinc ion binding
A	0015670	biological_process	carbon dioxide transport
A	0016829	molecular_function	lyase activity
A	0018820	molecular_function	cyanamide hydratase activity
A	0038166	biological_process	angiotensin-activated signaling pathway
A	0044070	biological_process	regulation of monoatomic anion transport
A	0045177	cellular_component	apical part of cell
A	0046872	molecular_function	metal ion binding
A	0051453	biological_process	regulation of intracellular pH
A	2001150	biological_process	positive regulation of dipeptide transmembrane transport
B	0004089	molecular_function	carbonate dehydratase activity
B	0005737	cellular_component	cytoplasm
B	0005886	cellular_component	plasma membrane
B	0008270	molecular_function	zinc ion binding
B	0015670	biological_process	carbon dioxide transport
B	0016829	molecular_function	lyase activity
B	0018820	molecular_function	cyanamide hydratase activity
B	0038166	biological_process	angiotensin-activated signaling pathway
B	0044070	biological_process	regulation of monoatomic anion transport
B	0045177	cellular_component	apical part of cell
B	0046872	molecular_function	metal ion binding
B	0051453	biological_process	regulation of intracellular pH
B	2001150	biological_process	positive regulation of dipeptide transmembrane transport
C	0004089	molecular_function	carbonate dehydratase activity
C	0005737	cellular_component	cytoplasm
C	0005886	cellular_component	plasma membrane
C	0008270	molecular_function	zinc ion binding
C	0015670	biological_process	carbon dioxide transport
C	0016829	molecular_function	lyase activity
C	0018820	molecular_function	cyanamide hydratase activity
C	0038166	biological_process	angiotensin-activated signaling pathway
C	0044070	biological_process	regulation of monoatomic anion transport
C	0045177	cellular_component	apical part of cell
C	0046872	molecular_function	metal ion binding
C	0051453	biological_process	regulation of intracellular pH
C	2001150	biological_process	positive regulation of dipeptide transmembrane transport
D	0004089	molecular_function	carbonate dehydratase activity
D	0005737	cellular_component	cytoplasm
D	0005886	cellular_component	plasma membrane
D	0008270	molecular_function	zinc ion binding
D	0015670	biological_process	carbon dioxide transport
D	0016829	molecular_function	lyase activity
D	0018820	molecular_function	cyanamide hydratase activity
D	0038166	biological_process	angiotensin-activated signaling pathway
D	0044070	biological_process	regulation of monoatomic anion transport
D	0045177	cellular_component	apical part of cell
D	0046872	molecular_function	metal ion binding
D	0051453	biological_process	regulation of intracellular pH
D	2001150	biological_process	positive regulation of dipeptide transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 268

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	THR198

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 268

Chain	Residue
B	HIS94
B	HIS96
B	HIS119
B	THR198

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 268

Chain	Residue
C	HIS96
C	HIS119
C	THR198
C	HIS94

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 268

Chain	Residue
D	HIS94
D	HIS96
D	HIS119
D	THR198

---

Functional Information from PROSITE/UniProt

site_id	PS00162
Number of Residues	17
Details	ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdrkkYaaELHLV

Chain	Residue	Details
A	SER105-VAL121

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15039588","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Site: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	512
Details	Domain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---