eF-site ID 1otx-B
PDB Code 1otx
Chain B

click to enlarge
Title Purine Nucleoside Phosphorylase M64V mutant
Classification TRANSFERASE
Compound Purine nucleoside phosphorylase
Source Escherichia coli (strain K12) (DEOD_ECOLI)
Sequence B:  ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN
NVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDF
GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRF
KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY
SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK
Description


Functional site

1) chain B
residue 20
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 248
source : AC2

2) chain B
residue 87
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 248
source : AC2

3) chain B
residue 89
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 248
source : AC2

4) chain B
residue 90
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 248
source : AC2

5) chain B
residue 43
type
sequence R
description BINDING SITE FOR RESIDUE PO4 C 249
source : AC3

6) chain B
residue 21
type catalytic
sequence D
description 375
source MCSA : MCSA2

7) chain B
residue 25
type catalytic
sequence A
description 375
source MCSA : MCSA2

8) chain B
residue 44
type catalytic
sequence G
description 375
source MCSA : MCSA2

9) chain B
residue 88
type catalytic
sequence V
description 375
source MCSA : MCSA2

10) chain B
residue 91
type catalytic
sequence C
description 375
source MCSA : MCSA2

11) chain B
residue 205
type catalytic
sequence H
description 375
source MCSA : MCSA2

12) chain B
residue 218
type catalytic
sequence Q
description 375
source MCSA : MCSA2

13) chain B
residue 5
type BINDING
sequence I
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

14) chain B
residue 21
type BINDING
sequence D
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

15) chain B
residue 25
type BINDING
sequence A
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

16) chain B
residue 88
type BINDING
sequence V
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

17) chain B
residue 44
type BINDING
sequence G
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

18) chain B
residue 180
type BINDING
sequence M
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

19) chain B
residue 204
type BINDING
sequence D
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

20) chain B
residue 218
type SITE
sequence Q
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

21) chain B
residue 27
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI7

22) chain B
residue 205
type ACT_SITE
sequence H
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572
source Swiss-Prot : SWS_FT_FI1


Display surface

Download
Links