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1QRG

A CLOSER LOOK AND THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005576cellular_componentextracellular region
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0043199molecular_functionsulfate binding
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
A0071890molecular_functionbicarbonate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 214
ChainResidue
AHIS81
AHIS117
AHIS122
AHOH288
AHOH289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10924115
ChainResidueDetails
AGLU62

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:10924115
ChainResidueDetails
AGLU84

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:10924115
ChainResidueDetails
AARG59
AGLN75
AASN202

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: 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
ChainResidueDetails
AHIS81
AHIS117
AHIS122

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 516
ChainResidueDetails
AGLU62electrostatic destabiliser, electrostatic stabiliser, proton acceptor, proton donor
AGLN75electrostatic stabiliser
AHIS81metal ligand
AGLU84proton acceptor
AHIS117metal ligand
AHIS122metal ligand
AASN202electrostatic stabiliser, increase electrophilicity

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PDB entries from 2024-03-27

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