3OTM

Crystal structures of wild-type gamma-carbonic anhydrase from Methanosarcina thermophila

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

Functional Information from PDB Data

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

Chain	Residue
A	HOH1
A	HIS81
A	HIS117
A	HIS122

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10924115

Chain	Residue	Details
A	GLY63

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:10924115

Chain	Residue	Details
A	THR85

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:10924115

Chain	Residue	Details
A	ASP76
A	VAL203
A	SER60

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site_id	SWS_FT_FI4
Number of Residues	3
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	GLY123
A	ALA82
A	GLN118

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 516

Chain	Residue	Details
A	GLY63	electrostatic destabiliser, electrostatic stabiliser, proton acceptor, proton donor
A	ASP76	electrostatic stabiliser
A	ALA82	metal ligand
A	THR85	proton acceptor
A	GLN118	metal ligand
A	GLY123	metal ligand
A	VAL203	electrostatic stabiliser, increase electrophilicity

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