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1V9E

Crystal Structure Analysis of Bovine Carbonic Anhydrase II

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
B0004089molecular_functioncarbonate dehydratase activity
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0015670biological_processcarbon dioxide transport
B0016829molecular_functionlyase activity
B0018820molecular_functioncyanamide hydratase activity
B0038166biological_processangiotensin-activated signaling pathway
B0044070biological_processregulation of monoatomic anion transport
B0045177cellular_componentapical part of cell
B0046872molecular_functionmetal ion binding
B0051453biological_processregulation of intracellular pH
B2001150biological_processpositive regulation of dipeptide transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 260
ChainResidue
AHIS93
AHIS95
AHIS118
ATHR197
AHOH462

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 260
ChainResidue
BHOH478
BHIS93
BHIS95
BHIS118
BTHR197

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15039588
ChainResidueDetails
APHE94
ATRP96
ALEU119
BPHE94
BTRP96
BLEU119

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR198
BTHR198

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AGLY7
AGLY62
AVAL67
BGLY7
BGLY62
BVAL67

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
AHIS2
BHIS2

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AILE165
ATHR172
BILE165
BTHR172

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR197
AHIS63

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BTHR197
BHIS63

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PDB entries from 2024-05-01

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