3MF3

Cobalt(II)-Substituted Haemophilus influenzae B-Carbonic Anhydrase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0008270	molecular_function	zinc ion binding
A	0015976	biological_process	carbon utilization
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
B	0004089	molecular_function	carbonate dehydratase activity
B	0008270	molecular_function	zinc ion binding
B	0015976	biological_process	carbon utilization
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
C	0004089	molecular_function	carbonate dehydratase activity
C	0008270	molecular_function	zinc ion binding
C	0015976	biological_process	carbon utilization
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
D	0004089	molecular_function	carbonate dehydratase activity
D	0008270	molecular_function	zinc ion binding
D	0015976	biological_process	carbon utilization
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
E	0004089	molecular_function	carbonate dehydratase activity
E	0008270	molecular_function	zinc ion binding
E	0015976	biological_process	carbon utilization
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
F	0004089	molecular_function	carbonate dehydratase activity
F	0008270	molecular_function	zinc ion binding
F	0015976	biological_process	carbon utilization
F	0016829	molecular_function	lyase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO A 230

Chain	Residue
A	CYS42
A	ASP44
A	HIS98
A	CYS101

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO B 230

Chain	Residue
B	CYS42
B	ASP44
B	HIS98
B	CYS101

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO C 230

Chain	Residue
C	ASP44
C	HIS98
C	CYS101
C	CYS42

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO D 230

Chain	Residue
D	CYS42
D	ASP44
D	HIS98
D	CYS101

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO E 230

Chain	Residue
E	CYS42
E	ASP44
E	HIS98
E	CYS101

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO F 230

Chain	Residue
F	CYS42
F	ASP44
F	HIS98
F	CYS101

---

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ACT E 222

Chain	Residue
C	THR73
C	ASP74
C	PHE75
D	ACT222
D	HOH238
E	THR73
E	ASP74
E	PHE75
E	ASN76
E	HOH246

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT D 222

Chain	Residue
D	THR73
D	ASP74
D	PHE75
E	ACT222
E	HOH246
F	THR73
F	ASP74
F	PHE75

---

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ACT B 222

Chain	Residue
A	ACT222
A	ACT222
A	HOH250
A	HOH250
B	THR73
B	THR73
B	ASP74
B	ASP74
B	PHE75
B	PHE75
B	ASN76

---

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ACT A 222

Chain	Residue
A	THR73
A	THR73
A	ASP74
A	ASP74
A	PHE75
A	PHE75
A	HOH250
A	HOH250
B	ACT222
B	ACT222
B	HOH229

---

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

---

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

Chain	Residue	Details
A	GLN82-GLY102

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16584170","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A8D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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