|
|
eF-site ID
|
1g1f-AB |
|
PDB Code
|
1g1f |
|
Chain
|
A, B |
|
click to enlarge
|
|
|
Title
|
CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A TRI-PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR)RK) FROM THE INSULIN RECEPTOR KINASE |
|
Classification
|
HYDROLASE, SIGNALING PROTEIN |
|
Compound
|
PROTEIN TYROSINE PHOSPHATASE 1B |
|
Source
|
null (1G1F) |
|
|
Sequence
|
A: |
EMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNK
NRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSY
ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKC
AQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELE
NLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRES
GSLSPEHGPVVVHASAGIGRSGTFCLADTCLLLMDKRKDP
SSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFI
MGDSSVQDQWKELSHED
|
| B: |
ETDXXR
|
|
|
Description
|
|
Functional site
|
|
|
1)
|
chain |
A |
| residue |
181 |
| type |
catalytic |
| sequence |
D
|
| description |
469
|
| source |
MCSA : MCSA1
|
|
|
2)
|
chain |
A |
| residue |
215 |
| type |
catalytic |
| sequence |
A
|
| description |
469
|
| source |
MCSA : MCSA1
|
|
|
3)
|
chain |
A |
| residue |
221 |
| type |
catalytic |
| sequence |
R
|
| description |
469
|
| source |
MCSA : MCSA1
|
|
|
4)
|
chain |
A |
| residue |
222 |
| type |
catalytic |
| sequence |
S
|
| description |
469
|
| source |
MCSA : MCSA1
|
|
|
5)
|
chain |
A |
| residue |
262 |
| type |
catalytic |
| sequence |
Q
|
| description |
469
|
| source |
MCSA : MCSA1
|
|
|
6)
|
chain |
A |
| residue |
215 |
| type |
CROSSLNK |
| sequence |
A
|
| 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
|
|
|
7)
|
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
|
|
|
8)
|
chain |
A |
| residue |
181 |
| type |
BINDING |
| sequence |
D
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
9)
|
chain |
A |
| residue |
215 |
| type |
BINDING |
| sequence |
A
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
10)
|
chain |
A |
| residue |
262 |
| type |
BINDING |
| sequence |
Q
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
11)
|
chain |
A |
| residue |
20 |
| type |
MOD_RES |
| sequence |
Y
|
| description |
Phosphotyrosine => ECO:0007744|PubMed:15592455
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
12)
|
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
|
|
|
13)
|
chain |
A |
| residue |
66 |
| type |
MOD_RES |
| sequence |
Y
|
| description |
Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
14)
|
chain |
A |
| residue |
215 |
| type |
MOD_RES |
| sequence |
A
|
| description |
S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477
|
| source |
Swiss-Prot : SWS_FT_FI8
|
|
|
15)
|
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
|
|
|
16)
|
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
|
|
|
17)
|
chain |
A |
| residue |
215 |
| type |
ACT_SITE |
| sequence |
A
|
| description |
Phosphocysteine intermediate
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
|