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Crystal structure of the gamma-carbonic anhydrase W19N mutant 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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 214
ChainResidue
AHIS81
AHIS117
AHIS122
AHOH215

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10924115
ChainResidueDetails
AASP61

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:10924115
ChainResidueDetails
ALEU83

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:10924115
ChainResidueDetails
AILE58
AVAL74
AVAL201

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
ALEU80
AALA116
AVAL121

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 516
ChainResidueDetails
AASP61electrostatic destabiliser, electrostatic stabiliser, proton acceptor, proton donor
AVAL74electrostatic stabiliser
ALEU80metal ligand
ALEU83proton acceptor
AALA116metal ligand
AVAL121metal ligand
AVAL201electrostatic stabiliser, increase electrophilicity

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PDB entries from 2024-07-31

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