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

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Title Crystal structure of Escherichia coli Orotate Phosphoribosyltransferase with an empty active site at 1.55 Angstrom resolution
Classification TRANSFERASE
Compound Orotate phosphoribosyltransferase
Source (PYRE_ECOLI)
Sequence AAA:  MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLF
NTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATT
TAVALAEHHDLDLPYCFNRKEAGNLVGSALQGRVMLVDDV
ITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISA
IQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKA
YREEFGV
BBB:  MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLF
NTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATT
TAVALAEHHDLDLPYCFNRKEAGNLVGSALQGRVMLVDDV
ITAIRESMEIIQANGATLAGVLISLDRQERGRGEISAIQE
VERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYRE
EFGV
Description


Functional site

1) 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

2) 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

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

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

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

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 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

10) chain BBB
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

11) 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

12) 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

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

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

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

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

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


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