eF-site ID 1rka-A
PDB Code 1rka
Chain A

click to enlarge
Title THE APO FORM OF E. COLI RIBOKINASE
Classification TRANSFERASE
Compound PROTEIN (RIBOKINASE)
Source Escherichia coli (strain K12) (RBSK_ECOLI)
Sequence A:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK
GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID
ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA
LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV
ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF
RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA
IAVTRKGAQPSVPWREEIDAFLDRQ
Description (1)  RIBOKINASE


Functional site

1) chain A
residue 255
type ACT_SITE
ligand
sequence D
description Proton acceptor. {ECO:0000255|HAMAP- Rule:MF_01987, ECO:0000305|PubMed:11786021}.
source Swiss-Prot : SWS_FT_FI1

2) chain A
residue 251
type METAL
ligand
sequence I
description Potassium; via carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021}
source Swiss-Prot : SWS_FT_FI2

3) chain A
residue 285
type METAL
ligand
sequence A
description Potassium; via carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021}
source Swiss-Prot : SWS_FT_FI2

4) chain A
residue 288
type METAL
ligand
sequence R
description Potassium; via carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021}
source Swiss-Prot : SWS_FT_FI2

5) chain A
residue 290
type METAL
ligand
sequence G
description Potassium; via carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021}
source Swiss-Prot : SWS_FT_FI2

6) chain A
residue 249
type METAL
ligand
sequence D
description Potassium. {ECO:0000255|HAMAP- Rule:MF_01987, ECO:0000305|PubMed:11786021}
source Swiss-Prot : SWS_FT_FI3

7) chain A
residue 294
type METAL
ligand
sequence S
description Potassium. {ECO:0000255|HAMAP- Rule:MF_01987, ECO:0000305|PubMed:11786021}
source Swiss-Prot : SWS_FT_FI3

8) chain A
residue 187
type BINDING
ligand
sequence N
description ATP. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409}.
source Swiss-Prot : SWS_FT_FI4

9) chain A
residue 279
type BINDING
ligand
sequence H
description ATP. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409}.
source Swiss-Prot : SWS_FT_FI4

10) chain A
residue 143
type BINDING
ligand
sequence E
description Substrate. {ECO:0000255|HAMAP- Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409}.
source Swiss-Prot : SWS_FT_FI5

11) chain A
residue 255
type BINDING
ligand
sequence D
description Substrate. {ECO:0000255|HAMAP- Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409}.
source Swiss-Prot : SWS_FT_FI5

12) chain A
residue 223-228
type NP_BIND
ligand
sequence TLGSRG
description ATP. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409}.
source Swiss-Prot : SWS_FT_FI6

13) chain A
residue 254-255
type NP_BIND
ligand
sequence GD
description ATP. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021}.
source Swiss-Prot : SWS_FT_FI7

14) chain A
residue 249-262
type prosite
ligand
sequence DTIAAGDTFNGALI
description pfkB family of carbohydrate kinases signature 2. [DNSK]-[PSTV]-x-[SAG](2)-[GD]-D-x(3)-[SAGV]-[AG]-[LIVMFYA]-[LIVMSTAP]
source prosite : PS00584

15) chain A
residue 254
type catalytic
ligand
sequence G
description Annotated By Reference To The Literature 1rk2
source CSA : CSA1

16) chain A
residue 255
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1rk2
source CSA : CSA1

17) chain A
residue 253
type catalytic
ligand
sequence A
description Annotated By Reference To The Literature 1rk2
source CSA : CSA1

18) chain A
residue 252
type catalytic
ligand
sequence A
description Annotated By Reference To The Literature 1rk2
source CSA : CSA1


Display surface

Download
Links