eF-site ID 1hb4-A
PDB Code 1hb4
Chain A

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Title ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN EXPOSED PRODUCT FROM ANAEROBIC ACOV FE COMPLEX)
Classification ANTIBIOTIC BIOSYNTHESIS
Compound ISOPENICILLIN N SYNTHASE
Source (IPNS_EMENI)
Sequence A:  SVSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFF
YAVNHGINVQRLSQKTKEFHMSITPEEKWDLAIRAYNKEH
QDQVRAGYYLSIPGKKAVESFCYLNPNFTPDHPRIQAKTP
THEVNVWPDETKHPGFQDFAEQYYWDVFGLSSALLKGYAL
ALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKT
AADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDI
EADDTGYLINCGSYMAHLTNNYYKAPIHRVKWVNAERQSL
PFFVNLGYDSVIDPFDPREPNGKSDREPLSYGDYLQNGLV
SLINKNGQT
Description


Functional site

1) chain A
residue 53
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A1333
source : AC1

2) chain A
residue 140
type
sequence D
description BINDING SITE FOR RESIDUE SO4 A1333
source : AC1

3) chain A
residue 141
type
sequence F
description BINDING SITE FOR RESIDUE SO4 A1333
source : AC1

4) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A1334
source : AC2

5) chain A
residue 216
type
sequence D
description BINDING SITE FOR RESIDUE FE2 A1334
source : AC2

6) chain A
residue 270
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A1334
source : AC2

7) chain A
residue 87
type
sequence R
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

8) chain A
residue 91
type
sequence Y
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

9) chain A
residue 183
type
sequence S
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

10) chain A
residue 187
type
sequence I
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

11) chain A
residue 189
type
sequence Y
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

12) chain A
residue 211
type
sequence F
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

13) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

14) chain A
residue 216
type
sequence D
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

15) chain A
residue 281
type
sequence S
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

16) chain A
residue 285
type
sequence F
description BINDING SITE FOR RESIDUE SCV A1332
source : AC3

17) chain A
residue 211
type catalytic
sequence F
description 145
source MCSA : MCSA1

18) chain A
residue 214
type catalytic
sequence H
description 145
source MCSA : MCSA1

19) chain A
residue 216
type catalytic
sequence D
description 145
source MCSA : MCSA1

20) chain A
residue 270
type catalytic
sequence H
description 145
source MCSA : MCSA1

21) chain A
residue 87
type BINDING
sequence R
description 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
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 91
type BINDING
sequence Y
description 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
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 189
type BINDING
sequence Y
description 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
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 216
type BINDING
sequence D
description 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
source Swiss-Prot : SWS_FT_FI1

25) chain A
residue 281
type BINDING
sequence S
description 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
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 270
type BINDING
sequence H
description 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
source Swiss-Prot : SWS_FT_FI4

27) chain A
residue 279
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00805
source Swiss-Prot : SWS_FT_FI5

28) chain A
residue 211
type SITE
sequence F
description Transition state stabilizer => ECO:0007744|PDB:1QJE
source Swiss-Prot : SWS_FT_FI6

29) chain A
residue 97-106
type prosite
sequence KKAVESFCYL
description IPNS_1 Isopenicillin N synthase signature 1. KkAveSfCYL
source prosite : PS00185

30) chain A
residue 250-263
type prosite
sequence LINCGSYMAHLTNN
description IPNS_2 Isopenicillin N synthase signature 2. LInCGSymAhlTnN
source prosite : PS00186

31) chain A
residue 183
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 214
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE
source Swiss-Prot : SWS_FT_FI3


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