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

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Title E. COLI RIBOKINASE IN COMPLEX WITH D-RIBOSE
Classification TRANSFERASE
Compound PROTEIN (RIBOKINASE)
Source Escherichia coli (strain K12) (RBSK_ECOLI)
Sequence A:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK
GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID
ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA
LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV
ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF
RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA
IAVTRKGAQPSVPWREEIDAFLDRQ
Description


Functional site

1) chain A
residue 14
type
sequence N
description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
source : RB1

2) chain A
residue 16
type
sequence D
description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
source : RB1

3) chain A
residue 42
type
sequence G
description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
source : RB1

4) chain A
residue 43
type
sequence K
description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
source : RB1

5) chain A
residue 46
type
sequence N
description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
source : RB1

6) chain A
residue 143
type
sequence E
description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
source : RB1

7) chain A
residue 255
type
sequence D
description RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
source : RB1

8) chain A
residue 98
type
sequence A
description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.
source : RB2

9) chain A
residue 100
type
sequence I
description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.
source : RB2

10) chain A
residue 110
type
sequence I
description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.
source : RB2

11) chain A
residue 112
type
sequence I
description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.
source : RB2

12) chain A
residue 251
type
sequence I
description RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.
source : RB2

13) chain A
residue 252
type catalytic
sequence A
description 663
source MCSA : MCSA1

14) chain A
residue 253
type catalytic
sequence A
description 663
source MCSA : MCSA1

15) chain A
residue 254
type catalytic
sequence G
description 663
source MCSA : MCSA1

16) chain A
residue 255
type catalytic
sequence D
description 663
source MCSA : MCSA1

17) chain A
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

18) chain A
residue 249-262
type prosite
sequence DTIAAGDTFNGALI
description PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTiAAGDtfnGALI
source prosite : PS00584

19) chain A
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

20) chain A
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

21) chain A
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

22) chain A
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

23) chain A
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

24) chain A
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

25) chain A
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

26) chain A
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

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

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

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

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

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

32) chain A
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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