eF-site ID 4qah-A
PDB Code 4qah
Chain A

click to enlarge
Title The second sphere residue T263 is important for function and activity of PTP1B through modulating WPD loop
Classification HYDROLASE
Compound Tyrosine-protein phosphatase non-receptor type 1
Source Homo sapiens (Human) (PTN1_HUMAN)
Sequence A:  MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKN
KNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRS
YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK
CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLEL
ENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE
SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKD
PSSVDIKKVLLEMRKFRMGLIQKADQLRFSYLAVIEGAKF
IMGDSSVQDQWKELSHEDL
Description


Functional site

1) chain A
residue 54
type
sequence H
description BINDING SITE FOR RESIDUE TRS A 301
source : AC1

2) chain A
residue 130
type
sequence E
description BINDING SITE FOR RESIDUE TRS A 301
source : AC1

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

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

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

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

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

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

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

10) 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

11) 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

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

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

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

15) chain A
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000269|PubMed:2546149
source Swiss-Prot : SWS_FT_FI4

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

17) 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

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

19) 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

20) 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

21) 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


Display surface

Download
Links