|
|
eF-site ID
|
1ygr-ABCD |
|
PDB Code
|
1ygr |
|
Chain
|
A, B, C, D |
|
click to enlarge
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Title
|
Crystal structure of the tandem phosphatase domain of RPTP CD45 |
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Classification
|
HYDROLASE |
|
Compound
|
CD45 Protein Tyrosine Phosphatase |
|
Source
|
null (CD3Z_HUMAN) |
|
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Sequence
|
A: |
EKQLXNVEPIHADILLETYKRKIADEGRPFLAEFQSIPRV
FSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDA
GSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRXIWEQ
KATVIVXVTRCEEGNRNKCAEYWPSXEEGTRAFGDVVVKI
NQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHG
VPEDPHLLLKLRRRVNAFSNFFSGPIVVHSSAGVGRTGTY
IGIDAXLEGLEAENKVDVYGYVVKLRRQRCLXVQVEAQYI
LIHQALVEYNQFGETEVNLSELHPYLHNXKKRDPPSEPSP
LEAEFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYN
RVPLKSKYINASFIXSYWKPEVXIAAQGPLKETIGDFWQX
IFQRKVKVIVXLTELKHGDQEICAQYWGEGKQTYGDIEVD
LKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQ
LPAEPKELISXIQVVKQKLPQKNHKSTPLLIHCRDGSQQT
GIFCALLNLLESAETEEVVDIFQVVKALRKARLGXVSTFE
QYQFLYDVIASTYP
|
| B: |
KQLXNVEPIHADILLETYKRKIADEGRPFLAEFQSIPRVF
SKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAG
SNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRXIWEQK
ATVIVXVTRCEEGNRNKCAEYWPSXEEGTRAFGDVVVKIN
QHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGV
PEDPHLLLKLRRRVNAFSNFFSGPIVVHSSAGVGRTGTYI
GIDAXLEGLEAENKVDVYGYVVKLRRQRCLXVQVEAQYIL
IHQALVEYNQFGETEVNLSELHPYLHNXKKRDPPSEPSPL
EAEFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYNR
VPLKHESKYINASFIXSYWKPEVXIAAQGPLKETIGDFWQ
XIFQRKVKVIVXLTELKHGDQEICAQYWGEGKQTYGDIEV
DLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVE
QLPAEPKELISXIQVVKQKLPKSTPLLIHCRDGSQQTGIF
CALLNLLESAETEEVVDIFQVVKALRKARLGXVSTFEQYQ
FLYDVIASTYPAQN
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| C: |
REEXDV
|
| D: |
REEXDV
|
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Description
|
|
Functional site
|
|
|
1)
|
chain |
A |
| residue |
952 |
| type |
MOD_RES |
| sequence |
V
|
| description |
Phosphoserine => ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
2)
|
chain |
B |
| residue |
952 |
| type |
MOD_RES |
| sequence |
V
|
| description |
Phosphoserine => ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
3)
|
chain |
D |
| residue |
2004 |
| type |
MOD_RES |
| sequence |
X
|
| description |
Phosphotyrosine => ECO:0007744|PubMed:12522270
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
4)
|
chain |
C |
| residue |
2004 |
| type |
MOD_RES |
| sequence |
X
|
| description |
Phosphotyrosine => ECO:0007744|PubMed:12522270
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
5)
|
chain |
A |
| residue |
1146 |
| type |
ACT_SITE |
| sequence |
D
|
| description |
Phosphocysteine intermediate => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
6)
|
chain |
B |
| residue |
1146 |
| type |
ACT_SITE |
| sequence |
D
|
| description |
Phosphocysteine intermediate => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
7)
|
chain |
A |
| residue |
874 |
| type |
BINDING |
| sequence |
E
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
8)
|
chain |
B |
| residue |
798 |
| type |
BINDING |
| sequence |
G
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
9)
|
chain |
A |
| residue |
798 |
| type |
BINDING |
| sequence |
G
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
10)
|
chain |
A |
| residue |
830 |
| type |
BINDING |
| sequence |
A
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
11)
|
chain |
B |
| residue |
830 |
| type |
BINDING |
| sequence |
A
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
12)
|
chain |
B |
| residue |
874 |
| type |
BINDING |
| sequence |
E
|
| description |
BINDING => ECO:0000250
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
13)
|
chain |
A |
| residue |
660 |
| type |
MOD_RES |
| sequence |
D
|
| description |
Phosphotyrosine => ECO:0000250|UniProtKB:P04157
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
14)
|
chain |
B |
| residue |
660 |
| type |
MOD_RES |
| sequence |
D
|
| description |
Phosphotyrosine => ECO:0000250|UniProtKB:P04157
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
|