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2Z2P

Crystal Structure of catalytically inactive H270A virginiamycin B lyase from Staphylococcus aureus with Quinupristin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0016829molecular_functionlyase activity
A0016835molecular_functioncarbon-oxygen lyase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0016829molecular_functionlyase activity
B0016835molecular_functioncarbon-oxygen lyase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A1001
ChainResidue
AGLU268
AGLU284

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A1003
ChainResidue
AASP67
AGLU69
ATRP71
AASP127

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DOL A2002
ChainResidue
AGLU268
BASN109
BASP151
BASN152
BTHR168
BGLU169
ALYS34
ATRP243
ASER266

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B1002
ChainResidue
BGLU268
BGLU284

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B1004
ChainResidue
BASP67
BGLU69
BASP127

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DOL B2003
ChainResidue
AASN152
BLYS34
BTRP243
BGLU268

site_idAC7
Number of Residues24
DetailsBINDING SITE FOR CHAIN C OF QUINUPRISTIN
ChainResidue
ATYR18
AHIS33
ATYR102
AMET117
ATYR142
ASER144
AASN159
AGLN160
AALA182
AGLY184
AVAL186
AILE201
AARG226
AHIS228
ATRP243
AGLU268
AGLU284
AMG1001
ADOL2002
BASP24
BSER66
BGLU106
BPRO108
BASN152

site_idAC8
Number of Residues22
DetailsBINDING SITE FOR CHAIN D OF QUINUPRISTIN
ChainResidue
AASP24
ASER66
AGLU106
APRO108
AASN152
BTYR18
BHIS33
BTYR102
BMET117
BTYR142
BSER144
BASN159
BGLN160
BALA182
BILE201
BARG226
BHIS228
BTRP243
BGLU268
BGLU284
BMG1002
BDOL2003

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AALA270
BALA270

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AHIS228
BHIS228

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17563376
ChainResidueDetails
AGLU268
AGLU284
BGLU268
BGLU284

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PDB entries from 2024-07-10

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