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6SKS

Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0015670biological_processcarbon dioxide transport
A0016829molecular_functionlyase activity
A0018820molecular_functioncyanamide hydratase activity
A0038166biological_processangiotensin-activated signaling pathway
A0044070biological_processregulation of monoatomic anion transport
A0045177cellular_componentapical part of cell
A0046872molecular_functionmetal ion binding
A0051453biological_processregulation of intracellular pH
A2001150biological_processpositive regulation of dipeptide transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CU A 301
ChainResidue
AHIS2
AHIS9
AHIS14
AASP18
AHOH571

site_idAC2
Number of Residues4
Detailsbinding site for residue CU A 302
ChainResidue
AASP150
AE68308
AHOH538
AHOH548

site_idAC3
Number of Residues5
Detailsbinding site for residue CU A 303
ChainResidue
AHIS3
ATRP4
AHIS63
AHOH401
AHOH575

site_idAC4
Number of Residues3
Detailsbinding site for residue CU A 304
ChainResidue
AHIS3
AHIS63
AHOH553

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 305
ChainResidue
AHIS93
AHIS95
AHIS118
AE68308

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL A 306
ChainResidue
ATYR6
ATRP243
AHOH433

site_idAC7
Number of Residues10
Detailsbinding site for residue GOL A 307
ChainResidue
AASN61
AHIS63
ASER64
AASN66
AGLN91
AHIS93
AE68308
AHOH424
AHOH503
AHOH506

site_idAC8
Number of Residues18
Detailsbinding site for residue E68 A 308
ChainResidue
AASP71
AVAL90
AGLN91
AHIS93
AHIS95
AHIS118
AVAL120
APHE129
AASP150
ALEU196
ATHR197
ATHR198
ATRP207
ACU302
AZN305
AGOL307
AHOH410
AHOH549

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdrkkYaaELHLV
ChainResidueDetails
ASER104-VAL120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS63

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15039588
ChainResidueDetails
AHIS93
AHIS95
AHIS118

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR197

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATYR6
AASN61
AASN66

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
ASER1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ASER164
ASER171

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PDB entries from 2024-07-17

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