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

1V9I

Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II

Functional Information from GO Data
ChainGOidnamespacecontents
C0004089molecular_functioncarbonate dehydratase activity
C0005737cellular_componentcytoplasm
C0005886cellular_componentplasma membrane
C0006730biological_processone-carbon metabolic process
C0008270molecular_functionzinc ion binding
C0015670biological_processcarbon dioxide transport
C0016829molecular_functionlyase activity
C0018820molecular_functioncyanamide hydratase activity
C0038166biological_processangiotensin-activated signaling pathway
C0044070biological_processregulation of monoatomic anion transport
C0045177cellular_componentapical part of cell
C0046872molecular_functionmetal ion binding
C0051453biological_processregulation of intracellular pH
C2001150biological_processpositive regulation of dipeptide transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 262
ChainResidue
CHIS95
CHIS97
CHIS120
CTHR199

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdrkkYaaELHLV
ChainResidueDetails
CSER106-VAL122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
CSER66

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15039588
ChainResidueDetails
CPHE96
CTRP98
CLEU121

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
CTHR200

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
CGLY9
CGLY64
CVAL69

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
CHIS4

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
CILE167
CTHR174

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
CTHR199
CHIS65

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon