eF-site ID 4ts9-ABC
PDB Code 4ts9
Chain A, B, C

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Title Crystal structure of wild type E. Coli purine nucleoside phosphorylase with 6 FMC molecules
Classification TRANSFERASE
Compound Purine nucleoside phosphorylase DeoD-type
Source ORGANISM_SCIENTIFIC: Escherichia coli;
Sequence A:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN
NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF
GVKKIIRVASCGAVLPHVKLRDVVIGMGACTDSKVNRIRF
KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY
SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK
B:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN
NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF
GVKKIIRVASCGAVLPHVKLRDVVIGMGACTDSKVNRIRF
KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY
SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK
C:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN
NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF
GVKKIIRVASCGAVLPHVKLRDVVIGMGACTDSKVNRIRF
KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY
SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK
Description


Functional site
1) chain A
residue 64
type
sequence M
description binding site for residue FMC A 300
source : AC1
2) chain A
residue 87
type
sequence R
description binding site for residue FMC A 300
source : AC1
3) chain A
residue 90
type
sequence S
description binding site for residue FMC A 300
source : AC1
4) chain A
residue 91
type
sequence C
description binding site for residue FMC A 300
source : AC1
5) chain A
residue 92
type
sequence G
description binding site for residue FMC A 300
source : AC1
6) chain A
residue 159
type
sequence F
description binding site for residue FMC A 300
source : AC1
7) chain A
residue 178
type
sequence V
description binding site for residue FMC A 300
source : AC1
8) chain A
residue 179
type
sequence E
description binding site for residue FMC A 300
source : AC1
9) chain A
residue 180
type
sequence M
description binding site for residue FMC A 300
source : AC1
10) chain A
residue 181
type
sequence E
description binding site for residue FMC A 300
source : AC1
11) chain A
residue 203
type
sequence S
description binding site for residue FMC A 300
source : AC1
12) chain A
residue 204
type
sequence D
description binding site for residue FMC A 300
source : AC1
13) chain A
residue 217
type
sequence R
description binding site for residue FMC A 300
source : AC1
14) chain C
residue 4
type
sequence H
description binding site for residue FMC A 300
source : AC1
15) chain C
residue 43
type
sequence R
description binding site for residue FMC A 300
source : AC1
16) chain A
residue 19
type
sequence P
description binding site for residue PO4 A 301
source : AC2
17) chain A
residue 20
type
sequence G
description binding site for residue PO4 A 301
source : AC2
18) chain A
residue 24
type
sequence R
description binding site for residue PO4 A 301
source : AC2
19) chain A
residue 87
type
sequence R
description binding site for residue PO4 A 301
source : AC2
20) chain A
residue 89
type
sequence A
description binding site for residue PO4 A 301
source : AC2
21) chain A
residue 90
type
sequence S
description binding site for residue PO4 A 301
source : AC2
22) chain C
residue 43
type
sequence R
description binding site for residue PO4 A 301
source : AC2
23) chain B
residue 20
type
sequence G
description binding site for residue PO4 B 301
source : AC3
24) chain B
residue 43
type
sequence R
description binding site for residue PO4 B 301
source : AC3
25) chain B
residue 87
type
sequence R
description binding site for residue PO4 B 301
source : AC3
26) chain B
residue 89
type
sequence A
description binding site for residue PO4 B 301
source : AC3
27) chain B
residue 90
type
sequence S
description binding site for residue PO4 B 301
source : AC3
28) chain B
residue 4
type
sequence H
description binding site for residue FMC B 302
source : AC4
29) chain B
residue 43
type
sequence R
description binding site for residue FMC B 302
source : AC4
30) chain B
residue 64
type
sequence M
description binding site for residue FMC B 302
source : AC4
31) chain B
residue 87
type
sequence R
description binding site for residue FMC B 302
source : AC4
32) chain B
residue 90
type
sequence S
description binding site for residue FMC B 302
source : AC4
33) chain B
residue 91
type
sequence C
description binding site for residue FMC B 302
source : AC4
34) chain B
residue 92
type
sequence G
description binding site for residue FMC B 302
source : AC4
35) chain B
residue 159
type
sequence F
description binding site for residue FMC B 302
source : AC4
36) chain B
residue 178
type
sequence V
description binding site for residue FMC B 302
source : AC4
37) chain B
residue 179
type
sequence E
description binding site for residue FMC B 302
source : AC4
38) chain B
residue 180
type
sequence M
description binding site for residue FMC B 302
source : AC4
39) chain B
residue 181
type
sequence E
description binding site for residue FMC B 302
source : AC4
40) chain B
residue 204
type
sequence D
description binding site for residue FMC B 302
source : AC4
41) chain B
residue 206
type
sequence I
description binding site for residue FMC B 302
source : AC4
42) chain A
residue 43
type
sequence R
description binding site for residue PO4 C 301
source : AC5
43) chain C
residue 20
type
sequence G
description binding site for residue PO4 C 301
source : AC5
44) chain C
residue 87
type
sequence R
description binding site for residue PO4 C 301
source : AC5
45) chain C
residue 89
type
sequence A
description binding site for residue PO4 C 301
source : AC5
46) chain C
residue 90
type
sequence S
description binding site for residue PO4 C 301
source : AC5
47) chain A
residue 4
type
sequence H
description binding site for residue FMC C 302
source : AC6
48) chain A
residue 43
type
sequence R
description binding site for residue FMC C 302
source : AC6
49) chain C
residue 87
type
sequence R
description binding site for residue FMC C 302
source : AC6
50) chain C
residue 90
type
sequence S
description binding site for residue FMC C 302
source : AC6
51) chain C
residue 91
type
sequence C
description binding site for residue FMC C 302
source : AC6
52) chain C
residue 92
type
sequence G
description binding site for residue FMC C 302
source : AC6
53) chain C
residue 159
type
sequence F
description binding site for residue FMC C 302
source : AC6
54) chain C
residue 178
type
sequence V
description binding site for residue FMC C 302
source : AC6
55) chain C
residue 179
type
sequence E
description binding site for residue FMC C 302
source : AC6
56) chain C
residue 180
type
sequence M
description binding site for residue FMC C 302
source : AC6
57) chain C
residue 181
type
sequence E
description binding site for residue FMC C 302
source : AC6
58) chain C
residue 204
type
sequence D
description binding site for residue FMC C 302
source : AC6
59) chain A
residue 61-76
type prosite
sequence GHGMGIPSCSIYTKEL
description PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL
source prosite : PS01232
60) chain A
residue 24
type catalytic
sequence R
description 375
source MCSA : MCSA1
61) chain A
residue 20
type catalytic
sequence G
description 375
source MCSA : MCSA1
62) chain A
residue 43
type catalytic
sequence R
description 375
source MCSA : MCSA1
63) chain A
residue 87
type catalytic
sequence R
description 375
source MCSA : MCSA1
64) chain A
residue 90
type catalytic
sequence S
description 375
source MCSA : MCSA1
65) chain A
residue 204
type catalytic
sequence D
description 375
source MCSA : MCSA1
66) chain A
residue 217
type catalytic
sequence R
description 375
source MCSA : MCSA1
67) chain B
residue 20
type catalytic
sequence G
description 375
source MCSA : MCSA2
68) chain B
residue 24
type catalytic
sequence R
description 375
source MCSA : MCSA2
69) chain B
residue 43
type catalytic
sequence R
description 375
source MCSA : MCSA2
70) chain B
residue 87
type catalytic
sequence R
description 375
source MCSA : MCSA2
71) chain B
residue 90
type catalytic
sequence S
description 375
source MCSA : MCSA2
72) chain B
residue 204
type catalytic
sequence D
description 375
source MCSA : MCSA2
73) chain B
residue 217
type catalytic
sequence R
description 375
source MCSA : MCSA2
74) chain C
residue 20
type catalytic
sequence G
description 375
source MCSA : MCSA3
75) chain C
residue 24
type catalytic
sequence R
description 375
source MCSA : MCSA3
76) chain C
residue 43
type catalytic
sequence R
description 375
source MCSA : MCSA3
77) chain C
residue 87
type catalytic
sequence R
description 375
source MCSA : MCSA3
78) chain C
residue 90
type catalytic
sequence S
description 375
source MCSA : MCSA3
79) chain C
residue 204
type catalytic
sequence D
description 375
source MCSA : MCSA3
80) chain C
residue 217
type catalytic
sequence R
description 375
source MCSA : MCSA3
81) chain A
residue 204
type ACT_SITE
sequence D
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572
source Swiss-Prot : SWS_FT_FI1
82) chain B
residue 204
type ACT_SITE
sequence D
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572
source Swiss-Prot : SWS_FT_FI1
83) chain C
residue 204
type ACT_SITE
sequence D
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572
source Swiss-Prot : SWS_FT_FI1
84) chain A
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
85) chain B
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
86) chain C
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
87) chain B
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
88) chain B
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
89) chain B
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
90) chain C
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
91) chain C
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
92) chain C
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
93) chain A
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
94) chain A
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
95) chain A
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
96) chain A
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
97) chain B
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
98) chain C
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
99) chain B
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
100) chain C
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
101) chain C
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
102) chain A
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
103) chain A
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
104) chain B
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
105) chain A
residue 217
type SITE
sequence R
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
106) chain B
residue 217
type SITE
sequence R
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
107) chain C
residue 217
type SITE
sequence R
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
108) chain A
residue 26
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI7
109) chain B
residue 26
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI7
110) chain C
residue 26
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI7

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