eF-site ID 1rk2-D
PDB Code 1rk2
Chain D

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Title E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP, SOLVED IN SPACE GROUP P212121
Classification TRANSFERASE
Compound RIBOKINASE
Source Escherichia coli (strain K12) (RBSK_ECOLI)
Sequence D:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK
GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID
ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA
LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV
ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF
RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA
IAVTRKGAQPSVPWREEIDAFLDRQ
Description


Functional site

1) chain D
residue 252
type catalytic
sequence A
description 663
source MCSA : MCSA4

2) chain D
residue 253
type catalytic
sequence A
description 663
source MCSA : MCSA4

3) chain D
residue 254
type catalytic
sequence G
description 663
source MCSA : MCSA4

4) chain D
residue 255
type catalytic
sequence D
description 663
source MCSA : MCSA4

5) chain D
residue 255
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI1

6) chain D
residue 14
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

7) chain D
residue 42
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

8) chain D
residue 143
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

9) chain D
residue 187
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

10) chain D
residue 223
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

11) chain D
residue 255
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

12) chain D
residue 279
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

13) chain D
residue 254
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021
source Swiss-Prot : SWS_FT_FI4

14) chain D
residue 249
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

15) chain D
residue 251
type BINDING
sequence I
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

16) chain D
residue 285
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

17) chain D
residue 288
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

18) chain D
residue 290
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

19) chain D
residue 294
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3


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