Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6SKV

Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH2)

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 Residues4
Detailsbinding site for residue ZN A 1000
ChainResidue
AHIS94
AHIS96
AHIS119
AE5Z1006

site_idAC2
Number of Residues5
Detailsbinding site for residue CU A 1001
ChainResidue
AHIS3
AHIS10
AHIS15
AASP19
AHOH1101

site_idAC3
Number of Residues4
Detailsbinding site for residue CU A 1002
ChainResidue
AHIS4
ATRP5
AHIS64
ACU1003

site_idAC4
Number of Residues4
Detailsbinding site for residue CU A 1003
ChainResidue
ATRP5
AHIS64
ACU1002
AHOH1124

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 1004
ChainResidue
ATYR7
ATRP244
AHOH1113

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 1005
ChainResidue
AASN62
ASER65
AASN67
AGLN92
AE5Z1006
AHOH1180

site_idAC7
Number of Residues15
Detailsbinding site for residue E5Z A 1006
ChainResidue
AGLU69
ATYR70
AVAL91
AGLN92
AHIS94
AHIS96
AHIS119
APHE130
ALEU197
ATHR198
ATHR199
ATRP208
AZN1000
AGOL1005
AHOH1166

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdrkkYaaELHLV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS64

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15039588
ChainResidueDetails
AHIS94
AHIS96
AHIS119

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR198

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATYR7
AASN62
AASN67

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
ASER2

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ASER165
ASER172

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon