eF-site ID 6taj-.AAA.BBB
PDB Code 6taj
Chain AAA, BBB

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Title Crystal structure of Escherichia coli Orotate Phosphoribosyltransferase in complex with Orotic acid 1.60 Angstrom resolution
Classification TRANSFERASE
Compound Orotate phosphoribosyltransferase
Source (PYRE_ECOLI)
Sequence AAA:  MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLF
NTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATT
TAVALAEHHDLDLPYCFNRKEGNLVGSALQGRVMLVDDVI
TAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISAI
QEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAY
REEFGV
BBB:  MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLF
NTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATT
TAVALAEHHDLDLPYCFNRNLVGSALQGRVMLVDDVITAG
TAIRESMEIIQANGATLAGVLISLDRQERGRGEISAIQEV
ERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREE
FGV
Description


Functional site

1) chain AAA
residue 120-132
type prosite
sequence VMLVDDVITAGTA
description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VMLVDDVITAGtA
source prosite : PS00103

2) chain AAA
residue 26
type BINDING
sequence K
description in other chain => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI1

3) chain AAA
residue 124
type BINDING
sequence D
description in other chain => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI1

4) chain BBB
residue 26
type BINDING
sequence K
description in other chain => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI1

5) chain BBB
residue 124
type BINDING
sequence D
description in other chain => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI1

6) chain AAA
residue 34
type BINDING
sequence F
description BINDING => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI2

7) chain AAA
residue 128
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI2

8) chain AAA
residue 156
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI2

9) chain BBB
residue 34
type BINDING
sequence F
description BINDING => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI2

10) chain BBB
residue 128
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI2

11) chain BBB
residue 156
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01208
source Swiss-Prot : SWS_FT_FI2

12) chain AAA
residue 72
type BINDING
sequence Y
description in other chain => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
source Swiss-Prot : SWS_FT_FI3

13) chain AAA
residue 100
type BINDING
sequence K
description in other chain => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
source Swiss-Prot : SWS_FT_FI3

14) chain BBB
residue 72
type BINDING
sequence Y
description in other chain => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
source Swiss-Prot : SWS_FT_FI3

15) chain AAA
residue 99
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
source Swiss-Prot : SWS_FT_FI4

16) chain BBB
residue 99
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002
source Swiss-Prot : SWS_FT_FI4


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