1THJ

CARBONIC ANHYDRASE FROM METHANOSARCINA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0005576	cellular_component	extracellular region
A	0008270	molecular_function	zinc ion binding
A	0016829	molecular_function	lyase activity
A	0043199	molecular_function	sulfate binding
A	0046872	molecular_function	metal ion binding
A	0050897	molecular_function	cobalt ion binding
A	0071890	molecular_function	bicarbonate binding
B	0004089	molecular_function	carbonate dehydratase activity
B	0005576	cellular_component	extracellular region
B	0008270	molecular_function	zinc ion binding
B	0016829	molecular_function	lyase activity
B	0043199	molecular_function	sulfate binding
B	0046872	molecular_function	metal ion binding
B	0050897	molecular_function	cobalt ion binding
B	0071890	molecular_function	bicarbonate binding
C	0004089	molecular_function	carbonate dehydratase activity
C	0005576	cellular_component	extracellular region
C	0008270	molecular_function	zinc ion binding
C	0016829	molecular_function	lyase activity
C	0043199	molecular_function	sulfate binding
C	0046872	molecular_function	metal ion binding
C	0050897	molecular_function	cobalt ion binding
C	0071890	molecular_function	bicarbonate binding

Functional Information from PDB Data

site_id	1
Number of Residues	5
Details	ACTIVE SITE 1, LOCATED BETWEEN A AND C CHAIN.

Chain	Residue
A	HIS81
A	HIS122
A	ZN214
C	HOH215
C	HIS117

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site_id	2
Number of Residues	5
Details	ACTIVE SITE 2, LOCATED BETWEEN B AND A CHAIN.

Chain	Residue
A	HIS117
B	HIS81
B	HIS122
B	ZN214
A	HOH215

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site_id	3
Number of Residues	5
Details	ACTIVE SITE 3, LOCATED BETWEEN C AND B CHAIN.

Chain	Residue
C	HIS81
C	HIS122
C	ZN214
B	HOH215
B	HIS117

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site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 214

Chain	Residue
A	HIS81
A	HIS122
C	HIS117
C	HOH215

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 214

Chain	Residue
A	HIS117
A	HOH215
B	HIS81
B	HIS122

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 214

Chain	Residue
B	HIS117
B	HOH215
C	HIS81
C	HIS122

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10924115

Chain	Residue	Details
A	GLU62
B	GLU62
C	GLU62

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:10924115

Chain	Residue	Details
A	GLU84
B	GLU84
C	GLU84

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:10924115

Chain	Residue	Details
A	ARG59
A	GLN75
A	ASN202
B	ARG59
B	GLN75
B	ASN202
C	ARG59
C	GLN75
C	ASN202

---

site_id	SWS_FT_FI4
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:10924115, ECO:0000269|PubMed:8665839, ECO:0007744|PDB:1QRG, ECO:0007744|PDB:1QRL, ECO:0007744|PDB:1QRM, ECO:0007744|PDB:1THJ

Chain	Residue	Details
A	HIS81
A	HIS117
A	HIS122
B	HIS81
B	HIS117
B	HIS122
C	HIS81
C	HIS117
C	HIS122

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1lxa

Chain	Residue	Details
A	GLY123

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1lxa

Chain	Residue	Details
B	GLY123

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site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1lxa

Chain	Residue	Details
C	GLY123

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site_id	MCSA1
Number of Residues	7
Details	M-CSA 516

Chain	Residue	Details
A	GLU62	electrostatic destabiliser, electrostatic stabiliser, proton acceptor, proton donor
A	GLN75	electrostatic stabiliser
A	HIS81	metal ligand
A	GLU84	proton acceptor
A	HIS117	metal ligand
A	HIS122	metal ligand
A	ASN202	electrostatic stabiliser, increase electrophilicity

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site_id	MCSA2
Number of Residues	7
Details	M-CSA 516

Chain	Residue	Details
B	GLU62	electrostatic destabiliser, electrostatic stabiliser, proton acceptor, proton donor
B	GLN75	electrostatic stabiliser
B	HIS81	metal ligand
B	GLU84	proton acceptor
B	HIS117	metal ligand
B	HIS122	metal ligand
B	ASN202	electrostatic stabiliser, increase electrophilicity

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site_id	MCSA3
Number of Residues	7
Details	M-CSA 516

Chain	Residue	Details
C	GLU62	electrostatic destabiliser, electrostatic stabiliser, proton acceptor, proton donor
C	GLN75	electrostatic stabiliser
C	HIS81	metal ligand
C	GLU84	proton acceptor
C	HIS117	metal ligand
C	HIS122	metal ligand
C	ASN202	electrostatic stabiliser, increase electrophilicity

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