eF-site ID 1yrl-C
PDB Code 1yrl
Chain C

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Title Escherichia coli ketol-acid reductoisomerase
Classification OXIDOREDUCTASE
Compound Ketol-acid reductoisomerase
Source Escherichia coli (strain K12) (ILVC_ECOLI)
Sequence C:  NYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVI
VGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKA
TENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQPLM
KDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVR
EEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHR
AGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVE
EGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAK
LRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWAN
DDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMI
AMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIA
RKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPG
DLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGYMT
DMKRIAV
Description (1)  Ketol-acid reductoisomerase(E.C.1.1.1.86)


Functional site

1) chain C
residue 11
type
ligand
sequence R
description BINDING SITE FOR RESIDUE SO4 C 4125
source : AC5

2) chain C
residue 12
type
ligand
sequence Q
description BINDING SITE FOR RESIDUE SO4 C 4125
source : AC5

3) chain C
residue 133
type ACT_SITE
ligand
sequence G
description {ECO:0000255|HAMAP-Rule:MF_00435}.
source Swiss-Prot : SWS_FT_FI21

4) chain C
residue 218
type METAL
ligand
sequence L
description Magnesium 1. {ECO:0000255|HAMAP- Rule:MF_00435, ECO:0000269|PubMed:23036858}
source Swiss-Prot : SWS_FT_FI22

5) chain C
residue 222
type METAL
ligand
sequence Q
description Magnesium 1. {ECO:0000255|HAMAP- Rule:MF_00435}
source Swiss-Prot : SWS_FT_FI23

6) chain C
residue 218
type METAL
ligand
sequence L
description Magnesium 2. {ECO:0000255|HAMAP- Rule:MF_00435, ECO:0000269|PubMed:23036858}
source Swiss-Prot : SWS_FT_FI24

7) chain C
residue 390
type METAL
ligand
sequence S
description Magnesium 2. {ECO:0000255|HAMAP- Rule:MF_00435, ECO:0000269|PubMed:23036858}
source Swiss-Prot : SWS_FT_FI24

8) chain C
residue 394
type METAL
ligand
sequence L
description Magnesium 2. {ECO:0000255|HAMAP- Rule:MF_00435, ECO:0000269|PubMed:23036858}
source Swiss-Prot : SWS_FT_FI24

9) chain C
residue 79
type BINDING
ligand
sequence W
description NADP. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858}.
source Swiss-Prot : SWS_FT_FI25

10) chain C
residue 159
type BINDING
ligand
sequence T
description NADP; via amide nitrogen. {ECO:0000255|HAMAP-Rule:MF_00435}.
source Swiss-Prot : SWS_FT_FI26

11) chain C
residue 69
type BINDING
ligand
sequence K
description NADP. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:9015391}.
source Swiss-Prot : SWS_FT_FI27

12) chain C
residue 415
type BINDING
ligand
sequence D
description Substrate. {ECO:0000255|HAMAP- Rule:MF_00435}.
source Swiss-Prot : SWS_FT_FI28

13) chain C
residue 77
type BINDING
ligand
sequence A
description NADP. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858, ECO:0000305|PubMed:9015391}.
source Swiss-Prot : SWS_FT_FI29

14) chain C
residue 46-49
type NP_BIND
ligand
sequence GAQG
description NADP. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858}.
source Swiss-Prot : SWS_FT_FI30

15) chain C
residue 109-111
type NP_BIND
ligand
sequence KQH
description NADP. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858}.
source Swiss-Prot : SWS_FT_FI30

16) chain C
residue 393
type catalytic
ligand
sequence E
description Annotated By Reference To The Literature 1yve
source CSA : CSA3

17) chain C
residue 383
type catalytic
ligand
sequence E
description Annotated By Reference To The Literature 1yve
source CSA : CSA7


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