eF-site ID 1cde-C
PDB Code 1cde
Chain C

click to enlarge
Title STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
Classification TRANSFERASE(FORMYL)
Compound PHOSPHORIBOSYL-GLYCINAMIDE FORMYLTRANSFERASE
Source Escherichia coli (strain K12) (PUR3_ECOLI)
Sequence C:  MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADA
FGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAP
DVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT
HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD
SEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG
QRLPPQGYA
Description


Functional site

1) chain C
residue 10
type
sequence N
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

2) chain C
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

3) chain C
residue 12
type
sequence S
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

4) chain C
residue 13
type
sequence N
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

5) chain C
residue 87
type
sequence G
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

6) chain C
residue 89
type
sequence M
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

7) chain C
residue 107
type
sequence I
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

8) chain C
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

9) chain C
residue 109
type
sequence P
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

10) chain C
residue 170
type
sequence Q
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

11) chain C
residue 173
type
sequence E
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

12) chain C
residue 89
type
sequence M
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

13) chain C
residue 90
type
sequence R
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

14) chain C
residue 91
type
sequence I
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

15) chain C
residue 92
type
sequence L
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

16) chain C
residue 97
type
sequence V
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

17) chain C
residue 106
type
sequence N
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

18) chain C
residue 139
type
sequence V
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

19) chain C
residue 140
type
sequence T
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

20) chain C
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

21) chain C
residue 142
type
sequence E
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

22) chain C
residue 144
type
sequence D
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

23) chain C
residue 106
type catalytic
sequence N
description 363
source MCSA : MCSA3

24) chain C
residue 108
type catalytic
sequence H
description 363
source MCSA : MCSA3

25) chain C
residue 135
type catalytic
sequence S
description 363
source MCSA : MCSA3

26) chain C
residue 144
type catalytic
sequence D
description 363
source MCSA : MCSA3

27) chain C
residue 108
type ACT_SITE
sequence H
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709
source Swiss-Prot : SWS_FT_FI1

28) chain C
residue 11
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI2

29) chain C
residue 89
type BINDING
sequence M
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI2

30) chain C
residue 64
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510
source Swiss-Prot : SWS_FT_FI3

31) chain C
residue 106
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510
source Swiss-Prot : SWS_FT_FI3

32) chain C
residue 140
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI4

33) chain C
residue 170
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI4

34) chain C
residue 144
type SITE
sequence D
description Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709
source Swiss-Prot : SWS_FT_FI5


Display surface

Download
Links