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

3QY1

1.54A Resolution Crystal Structure of a Beta-Carbonic Anhydrase from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
A0015976biological_processcarbon utilization
A0016829molecular_functionlyase activity
A0034599biological_processcellular response to oxidative stress
A0046872molecular_functionmetal ion binding
A0071244biological_processcellular response to carbon dioxide
B0004089molecular_functioncarbonate dehydratase activity
B0005737cellular_componentcytoplasm
B0008270molecular_functionzinc ion binding
B0015976biological_processcarbon utilization
B0016829molecular_functionlyase activity
B0034599biological_processcellular response to oxidative stress
B0046872molecular_functionmetal ion binding
B0071244biological_processcellular response to carbon dioxide
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 221
ChainResidue
ACYS42
AASP44
AHIS98
ACYS101

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 221
ChainResidue
BCYS42
BASP44
BHIS98
BCYS101

Functional Information from PROSITE/UniProt
site_idPS00704
Number of Residues8
DetailsPROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CSDSRVpA
ChainResidueDetails
ACYS42-ALA49

site_idPS00705
Number of Residues21
DetailsPROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QYAVdvLevehIIIcGHsgCG
ChainResidueDetails
AGLN82-GLY102

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon