eF-site ID 1qfe-AB
PDB Code 1qfe
Chain A, B

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Title THE STRUCTURE OF TYPE I 3-DEHYDROQUINATE DEHYDRATASE FROM SALMONELLA TYPHI
Classification LYASE
Compound PROTEIN (3-DEHYDROQUINATE DEHYDRATASE)
Source ORGANISM_SCIENTIFIC: Salmonella typhi;
Sequence A:  MKTVTVKNLIIGEGMPKIIVSLMGRDINSVKAEALAYREA
TFDILEWRVDHFMDIASTQSVLTAARVIRDAMPDIPLLFT
FRSAKEGGEQTITTQHYLTLNRAAIDSGLVDMIDLELFTG
DADVKATVDYAHAHNVYVVMSNHDFHQTPSAEEMVSRLRK
MQALGADIPKIAVMPQSKHDVLTLLTATLEMQQHYADRPV
ITMSMAKEGVISRLAGEVFGSAATFGAVKQASAPGQIAVN
DLRSVLMILHNA
B:  MKTVTVKNLIIGEGMPKIIVSLMGRDINSVKAEALAYREA
TFDILEWRVDHFMDIASTQSVLTAARVIRDAMPDIPLLFT
FRSAKEGGEQTITTQHYLTLNRAAIDSGLVDMIDLELFTG
DADVKATVDYAHAHNVYVVMSNHDFHQTPSAEEMVSRLRK
MQALGADIPKIAVMPQSKHDVLTLLTATLEMQQHYADRPV
ITMSMAKEGVISRLAGEVFGSAATFGAVKQASAPGQIAVN
DLRSVLMILHNA
Description


Functional site
1) chain A
residue 170
type
sequence K
description LYS 170 FORMS THE IMINE INTERMEDIATE WITH THE AID OF HIS 143 ARG 213 INTERACTS WITH THE CARBOXYL GROUP OF THE 3-DEHYDROQUINATE SUBSTRATE.
source : ASR
2) chain A
residue 143
type
sequence H
description LYS 170 FORMS THE IMINE INTERMEDIATE WITH THE AID OF HIS 143 ARG 213 INTERACTS WITH THE CARBOXYL GROUP OF THE 3-DEHYDROQUINATE SUBSTRATE.
source : ASR
3) chain A
residue 213
type
sequence R
description LYS 170 FORMS THE IMINE INTERMEDIATE WITH THE AID OF HIS 143 ARG 213 INTERACTS WITH THE CARBOXYL GROUP OF THE 3-DEHYDROQUINATE SUBSTRATE.
source : ASR
4) chain A
residue 21
type
sequence S
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
5) chain A
residue 46
type
sequence E
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
6) chain A
residue 48
type
sequence R
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
7) chain A
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
8) chain A
residue 143
type
sequence H
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
9) chain A
residue 170
type
sequence K
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
10) chain A
residue 203
type
sequence M
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
11) chain A
residue 213
type
sequence R
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
12) chain A
residue 225
type
sequence F
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
13) chain A
residue 232
type
sequence S
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
14) chain A
residue 233
type
sequence A
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
15) chain A
residue 236
type
sequence Q
description BINDING SITE FOR RESIDUE DHS A 301
source : AC1
16) chain B
residue 21
type
sequence S
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
17) chain B
residue 46
type
sequence E
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
18) chain B
residue 48
type
sequence R
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
19) chain B
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
20) chain B
residue 143
type
sequence H
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
21) chain B
residue 170
type
sequence K
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
22) chain B
residue 203
type
sequence M
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
23) chain B
residue 213
type
sequence R
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
24) chain B
residue 225
type
sequence F
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
25) chain B
residue 232
type
sequence S
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
26) chain B
residue 233
type
sequence A
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
27) chain B
residue 236
type
sequence Q
description BINDING SITE FOR RESIDUE DHS B 301
source : AC2
28) chain A
residue 86
type catalytic
sequence E
description 54
source MCSA : MCSA1
29) chain A
residue 143
type catalytic
sequence H
description 54
source MCSA : MCSA1
30) chain A
residue 170
type catalytic
sequence K
description 54
source MCSA : MCSA1
31) chain B
residue 86
type catalytic
sequence E
description 54
source MCSA : MCSA2
32) chain B
residue 143
type catalytic
sequence H
description 54
source MCSA : MCSA2
33) chain B
residue 170
type catalytic
sequence K
description 54
source MCSA : MCSA2
34) chain A
residue 114-144
type prosite
sequence DLELFTGDADVKATVDYAHAHNVYVVMSNHD
description DEHYDROQUINASE_I Dehydroquinase class I active site. DLELftgdadvkatvdyahahnvyVVmSNHD
source prosite : PS01028
35) chain A
residue 143
type ACT_SITE
sequence H
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000305|PubMed:24957267
source Swiss-Prot : SWS_FT_FI1
36) chain B
residue 143
type ACT_SITE
sequence H
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000305|PubMed:24957267
source Swiss-Prot : SWS_FT_FI1
37) chain A
residue 170
type ACT_SITE
sequence K
description Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491
source Swiss-Prot : SWS_FT_FI2
38) chain B
residue 170
type ACT_SITE
sequence K
description Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491
source Swiss-Prot : SWS_FT_FI2
39) chain A
residue 21
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491
source Swiss-Prot : SWS_FT_FI3
40) chain A
residue 232
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491
source Swiss-Prot : SWS_FT_FI3
41) chain B
residue 21
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491
source Swiss-Prot : SWS_FT_FI3
42) chain B
residue 232
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491
source Swiss-Prot : SWS_FT_FI3
43) chain A
residue 46
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267
source Swiss-Prot : SWS_FT_FI4
44) chain A
residue 213
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267
source Swiss-Prot : SWS_FT_FI4
45) chain A
residue 236
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267
source Swiss-Prot : SWS_FT_FI4
46) chain B
residue 46
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267
source Swiss-Prot : SWS_FT_FI4
47) chain B
residue 213
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267
source Swiss-Prot : SWS_FT_FI4
48) chain B
residue 236
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267
source Swiss-Prot : SWS_FT_FI4
49) chain A
residue 82
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352
source Swiss-Prot : SWS_FT_FI5
50) chain B
residue 82
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352
source Swiss-Prot : SWS_FT_FI5

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