eF-site ID 4tti-F
PDB Code 4tti
Chain F

click to enlarge
Title Crystal structure of double mutant E. Coli purine nucleoside phosphorylase with 4 FMC molecules
Classification TRANSFERASE
Compound Purine nucleoside phosphorylase DeoD-type
Source (DEOD_ECOLI)
Sequence F:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN
NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF
GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRF
KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY
SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSAHIRTHEQTTAAEAQTTFNDMIKIALESVLLGDK
Description


Functional site

1) chain F
residue 4
type
sequence H
description binding site for residue FMC C 301
source : AC4

2) chain F
residue 43
type
sequence R
description binding site for residue FMC C 301
source : AC4

3) chain F
residue 43
type
sequence R
description binding site for residue PO4 C 302
source : AC5

4) chain F
residue 64
type
sequence M
description binding site for residue FMC F 301
source : AD4

5) chain F
residue 87
type
sequence R
description binding site for residue FMC F 301
source : AD4

6) chain F
residue 90
type
sequence S
description binding site for residue FMC F 301
source : AD4

7) chain F
residue 91
type
sequence C
description binding site for residue FMC F 301
source : AD4

8) chain F
residue 92
type
sequence G
description binding site for residue FMC F 301
source : AD4

9) chain F
residue 159
type
sequence F
description binding site for residue FMC F 301
source : AD4

10) chain F
residue 178
type
sequence V
description binding site for residue FMC F 301
source : AD4

11) chain F
residue 179
type
sequence E
description binding site for residue FMC F 301
source : AD4

12) chain F
residue 180
type
sequence M
description binding site for residue FMC F 301
source : AD4

13) chain F
residue 181
type
sequence E
description binding site for residue FMC F 301
source : AD4

14) chain F
residue 203
type
sequence S
description binding site for residue FMC F 301
source : AD4

15) chain F
residue 19
type
sequence P
description binding site for residue PO4 F 302
source : AD5

16) chain F
residue 20
type
sequence G
description binding site for residue PO4 F 302
source : AD5

17) chain F
residue 24
type
sequence R
description binding site for residue PO4 F 302
source : AD5

18) chain F
residue 87
type
sequence R
description binding site for residue PO4 F 302
source : AD5

19) chain F
residue 89
type
sequence G
description binding site for residue PO4 F 302
source : AD5

20) chain F
residue 90
type
sequence S
description binding site for residue PO4 F 302
source : AD5

21) chain F
residue 222
type
sequence N
description binding site for residue SO4 F 303
source : AD6

22) chain F
residue 43
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
source Swiss-Prot : SWS_FT_FI4

23) chain F
residue 179
type BINDING
sequence E
description in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
source Swiss-Prot : SWS_FT_FI5

24) chain F
residue 203
type BINDING
sequence S
description in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
source Swiss-Prot : SWS_FT_FI5

25) chain F
residue 20
type catalytic
sequence G
description 375
source MCSA : MCSA6

26) chain F
residue 24
type catalytic
sequence R
description 375
source MCSA : MCSA6

27) chain F
residue 43
type catalytic
sequence R
description 375
source MCSA : MCSA6

28) chain F
residue 87
type catalytic
sequence R
description 375
source MCSA : MCSA6

29) chain F
residue 90
type catalytic
sequence S
description 375
source MCSA : MCSA6

30) chain F
residue 204
type catalytic
sequence A
description 375
source MCSA : MCSA6

31) chain F
residue 217
type catalytic
sequence A
description 375
source MCSA : MCSA6

32) chain F
residue 204
type ACT_SITE
sequence A
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572
source Swiss-Prot : SWS_FT_FI1

33) chain F
residue 217
type SITE
sequence A
description Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572
source Swiss-Prot : SWS_FT_FI6

34) chain F
residue 26
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI7

35) chain F
residue 4
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
source Swiss-Prot : SWS_FT_FI2

36) chain F
residue 20
type BINDING
sequence G
description in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
source Swiss-Prot : SWS_FT_FI3

37) chain F
residue 24
type BINDING
sequence R
description in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
source Swiss-Prot : SWS_FT_FI3

38) chain F
residue 87
type BINDING
sequence R
description in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
source Swiss-Prot : SWS_FT_FI3


Display surface

Download
Links