eF-site ID 5ejg-ABCD
PDB Code 5ejg
Chain A, B, C, D

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Title Crystal structure of NAD kinase P252D mutant from Listeria monocytogenes
Classification TRANSFERASE
Compound NAD kinase 1
Source Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) (NADK1_LISMO)
Sequence A:  MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVI
SIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKKEATYLALNEST
VKSPFVVDVVINDIHFERFRGDGLCMSTPSGTTAYNKSLG
GALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVS
LQPVDKDFQISVDHLSILHRDVQEIRYEVSAKKIHFARFR
SFDFWRRVHDSFI
B:  MKYMITSKGDEKSDLLRLNMIAGFGEYEYDDVEPEIVISI
GGDGTFLSAFHQYEERLDEIAFIGIHTFYADWRPAEADKL
VKLLAKGYQKVSYPLLKTTVKYEATYLALNESTVKSSGGP
FVVDVVINDIHFERFRGDGLCMSTPSGTTAYNKSLGGALM
HPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPV
NDKDFQISVDHLSILHRDVQEIRYEVSAKKIHFARFRSFD
FWRRVHDSFIEDLE
C:  SDLLRLNMIAGFMEYDDEPEIVISIGGDGTFLSAFHIAFI
GIHTFYADWADKLVKLLYQKVSYPLLKTTVKKEATYLALN
ESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGTTA
YNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFP
KHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSAKK
IHFARFFDFWRRVHDSFI
D:  KYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVIS
IGGDGTFLSAFHQYEERLDEIAFIGIHTGGFYADWRPAEA
DKLVKLLAKVSYPLLKTTVKYKKEATYLALNESTVKSSGG
PFVVDVVINDIHFERFRGDGLCMSTPSGTTAYNKSLGGAL
MHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQP
VNDKDFQISVDHLSILHRDVQEIRYEVSAKKIHFARFRSF
DFWRRVHDSFIE
Description


Functional site
1) chain A
residue 45
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI1
2) chain B
residue 45
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI1
3) chain C
residue 45
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI1
4) chain D
residue 45
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI1
5) chain A
residue 45
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
6) chain B
residue 158
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
7) chain B
residue 161
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
8) chain B
residue 223
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
9) chain C
residue 45
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
10) chain C
residue 46
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
11) chain C
residue 122
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
12) chain C
residue 158
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
13) chain C
residue 161
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
14) chain C
residue 223
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
15) chain D
residue 45
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
16) chain A
residue 46
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
17) chain D
residue 46
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
18) chain D
residue 122
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
19) chain D
residue 158
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
20) chain D
residue 161
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
21) chain D
residue 223
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
22) chain A
residue 122
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
23) chain A
residue 158
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
24) chain A
residue 161
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
25) chain A
residue 223
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
26) chain B
residue 45
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
27) chain B
residue 46
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
28) chain B
residue 122
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2
29) chain A
residue 148
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361
source Swiss-Prot : SWS_FT_FI3
30) chain B
residue 148
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361
source Swiss-Prot : SWS_FT_FI3
31) chain C
residue 148
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361
source Swiss-Prot : SWS_FT_FI3
32) chain D
residue 148
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361
source Swiss-Prot : SWS_FT_FI3
33) chain A
residue 150
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:17686780
source Swiss-Prot : SWS_FT_FI4
34) chain B
residue 150
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:17686780
source Swiss-Prot : SWS_FT_FI4
35) chain C
residue 150
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:17686780
source Swiss-Prot : SWS_FT_FI4
36) chain D
residue 150
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:17686780
source Swiss-Prot : SWS_FT_FI4

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