eF-site ID 1hn9-AB
PDB Code 1hn9
Chain A, B

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Title CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III
Classification TRANSFERASE
Compound BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III
Source Escherichia coli (strain K12) (FABH_ECOLI)
Sequence A:  MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIR
ERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVAT
TSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALS
VADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDG
AGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPE
NSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDW
LVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASV
PCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF
B:  MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIR
ERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVAT
TSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALS
VADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDG
AGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPE
NSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDW
LVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASV
PCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF
Description


Functional site

1) chain A
residue 4
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

2) chain A
residue 169
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

3) chain A
residue 170
type
sequence E
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

4) chain A
residue 171
type
sequence E
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

5) chain B
residue 1004
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 1350
source : AC2

6) chain B
residue 1169
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 1350
source : AC2

7) chain B
residue 1170
type
sequence E
description BINDING SITE FOR RESIDUE PO4 B 1350
source : AC2

8) chain B
residue 1171
type
sequence E
description BINDING SITE FOR RESIDUE PO4 B 1350
source : AC2

9) chain A
residue 112
type ACT_SITE
sequence C
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:10593943, ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824
source Swiss-Prot : SWS_FT_FI1

10) chain A
residue 244
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:10593943, ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824
source Swiss-Prot : SWS_FT_FI1

11) chain A
residue 274
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:10593943, ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824
source Swiss-Prot : SWS_FT_FI1

12) chain B
residue 1112
type ACT_SITE
sequence C
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:10593943, ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824
source Swiss-Prot : SWS_FT_FI1

13) chain B
residue 1244
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:10593943, ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824
source Swiss-Prot : SWS_FT_FI1

14) chain B
residue 1274
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:10593943, ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824
source Swiss-Prot : SWS_FT_FI1


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