eF-site ID 2vew-A
PDB Code 2vew
Chain A

click to enlarge
Title CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR
Classification HYDROLASE
Compound TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1
Source (PTN1_HUMAN)
Sequence A:  MEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKN
RNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYI
LTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCA
QYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELEN
LTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESG
SLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPS
SVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIM
GDSSVQDQWKELSHEDL
Description (1)  TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1 (E.C.3.1.3.48)


Functional site

1) chain A
residue 46
type
sequence Y
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

2) chain A
residue 47
type
sequence R
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

3) chain A
residue 48
type
sequence D
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

4) chain A
residue 49
type
sequence V
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

5) chain A
residue 181
type
sequence D
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

6) chain A
residue 182
type
sequence F
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

7) chain A
residue 215
type
sequence C
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

8) chain A
residue 216
type
sequence S
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

9) chain A
residue 217
type
sequence A
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

10) chain A
residue 219
type
sequence I
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

11) chain A
residue 220
type
sequence G
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

12) chain A
residue 221
type
sequence R
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

13) chain A
residue 262
type
sequence Q
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

14) chain A
residue 266
type
sequence Q
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

15) chain A
residue 293
type
sequence E
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

16) chain A
residue 294
type
sequence L
description BINDING SITE FOR RESIDUE IZ3 A1299
source : AC1

17) chain A
residue 215
type CROSSLNK
sequence C
description N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339
source Swiss-Prot : SWS_FT_FI10

18) chain A
residue 216
type CROSSLNK
sequence S
description N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339
source Swiss-Prot : SWS_FT_FI10

19) chain A
residue 20
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI5

20) chain A
residue 50
type MOD_RES
sequence S
description Phosphoserine; by PKB/AKT1, CLK1 and CLK2 => ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:11579209, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

21) chain A
residue 66
type MOD_RES
sequence Y
description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745
source Swiss-Prot : SWS_FT_FI7

22) chain A
residue 215
type MOD_RES
sequence C
description S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477
source Swiss-Prot : SWS_FT_FI8

23) chain A
residue 243
type MOD_RES
sequence S
description Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872
source Swiss-Prot : SWS_FT_FI9

24) chain A
residue 242
type MOD_RES
sequence S
description Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872
source Swiss-Prot : SWS_FT_FI9

25) chain A
residue 213-223
type prosite
sequence VHCSAGIGRSG
description TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRSG
source prosite : PS00383

26) chain A
residue 181
type catalytic
sequence D
description 469
source MCSA : MCSA1

27) chain A
residue 215
type catalytic
sequence C
description 469
source MCSA : MCSA1

28) chain A
residue 221
type catalytic
sequence R
description 469
source MCSA : MCSA1

29) chain A
residue 222
type catalytic
sequence S
description 469
source MCSA : MCSA1

30) chain A
residue 262
type catalytic
sequence Q
description 469
source MCSA : MCSA1

31) chain A
residue 215
type ACT_SITE
sequence C
description Phosphocysteine intermediate
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 181
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 262
type BINDING
sequence Q
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 215
type BINDING
sequence C
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3


Display surface

Download
Links