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7SEV

Crystal structure of E coli contaminant protein YadF co-purified with a plant protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0015976biological_processcarbon utilization
A0016829molecular_functionlyase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
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. QYAVdvLevehIIIcGHygCG
ChainResidueDetails
AGLN82-GLY102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11316870, ECO:0007744|PDB:1I6O, ECO:0007744|PDB:1I6P
ChainResidueDetails
ACYS42
AASP44
AHIS98
ACYS101

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 517
ChainResidueDetails
ACYS42metal ligand
AASP44metal ligand, proton acceptor
AARG46electrostatic stabiliser, increase basicity
AHIS98metal ligand
ACYS101metal ligand

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PDB entries from 2024-07-24

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