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1OBN

ISOPENICILLIN N SYNTHASE aminoadipoyl-cysteinyl-aminobutyrate-FE-NO COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009058biological_processbiosynthetic process
A0016216molecular_functionisopenicillin-N synthase activity
A0016491molecular_functionoxidoreductase activity
A0017000biological_processantibiotic biosynthetic process
A0031418molecular_functionL-ascorbic acid binding
A0042318biological_processpenicillin biosynthetic process
A0044249biological_processcellular biosynthetic process
A0044283biological_processsmall molecule biosynthetic process
A0046872molecular_functionmetal ion binding
A1901362biological_processorganic cyclic compound biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 A1333
ChainResidue
AHIS214
AASP216
AHIS270
AASV1332
AHOA1334
AHOH2182

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A1335
ChainResidue
AHOH2127
AHOH2134
AHOH2253
AHOH2254
AHOH2255
AARG53
AASP140
APHE141

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ASV A1332
ChainResidue
AARG87
ATYR91
ASER183
AILE187
ATYR189
APHE211
AHIS214
AASP216
ASER281
APHE285
AFE21333
AHOA1334
AHOH2249
AHOH2250
AHOH2251
AHOH2252

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HOA A1334
ChainResidue
AHIS214
AHIS270
AASV1332
AFE21333
AHOH2182

Functional Information from PROSITE/UniProt
site_idPS00185
Number of Residues10
DetailsIPNS_1 Isopenicillin N synthase signature 1. KkAveSfCYL
ChainResidueDetails
ALYS97-LEU106

site_idPS00186
Number of Residues14
DetailsIPNS_2 Isopenicillin N synthase signature 2. LInCGSymAhlTnN
ChainResidueDetails
ALEU250-ASN263

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS
ChainResidueDetails
AARG87
ATYR91
ATYR189
AASP216
ASER281

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS
ChainResidueDetails
ASER183

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE
ChainResidueDetails
AHIS214

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ, ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2, ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4, ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1, ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN, ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW, ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04, ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06, ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X, ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI, ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4, ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB, ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP, ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1, ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60, ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU, ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3
ChainResidueDetails
AHIS270

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805
ChainResidueDetails
AARG279

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0007744|PDB:1QJE
ChainResidueDetails
APHE211

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 145
ChainResidueDetails
APHE211polar/non-polar interaction, steric role
AHIS214metal ligand
AASP216metal ligand
AHIS270metal ligand

218853

PDB entries from 2024-04-24

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