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1ILZ

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 6.1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004620molecular_functionphospholipase activity
A0006629biological_processlipid metabolic process
A0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues45
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
AGLN1-LEU32
AGLY80-ASN85
AALA129-GLY130
AGLY167-ASN168
AGLY204-ASP205
AILE231-VAL235
AASP267-PHE269

site_idSWS_FT_FI2
Number of Residues133
DetailsTRANSMEM: Beta stranded
ChainResidueDetails
ATYR33-THR45
AGLY222-PRO230
AARG236-TYR245
AASN255-ASN266
AASP65-ARG79
ASER86-TRP98
APHE109-PHE128
ATRP131-SER144
ASER154-ASN166
ATRP169-VAL178
ALEU197-LEU203
AALA206-TYR214

site_idSWS_FT_FI3
Number of Residues66
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
ASER46-LYS64
AGLN99-PRO108
AASN145-ARG153
AVAL179-GLN196
AASN215-GLY221
AGLY246-PHE254

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AHIS142

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:2040286
ChainResidueDetails
ASER144

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: in dimeric form
ChainResidueDetails
ASER106
AARG147
ASER152

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: in monomeric form
ChainResidueDetails
AASP184

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 650
ChainResidueDetails
ASER106metal ligand
AHIS142proton acceptor, proton donor
ASER144covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AGLY146electrostatic stabiliser
AARG147metal ligand
ASER152metal ligand
AALA156electrostatic stabiliser, increase basicity

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PDB entries from 2024-04-24

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