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1WCH

Crystal structure of PTPL1 human tyrosine phosphatase mutated in colorectal cancer - evidence for a second phosphotyrosine substrate recognition pocket

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PO4 A3478
ChainResidue
AASP2378
AHOH3260
AHOH3275
ACYS2408
ASER2409
AALA2410
AGLY2411
AILE2412
AGLY2413
AARG2414
AGLN2452

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A3479
ChainResidue
ASER2334
AASN2335
AARG2336
AHOH3277

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A3480
ChainResidue
AGLN2310
AGLU2311
AASN2372
ATHR2374
AHOH3278
AHOH3279
AHOH3280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues254
DetailsDomain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsRegion: {"description":"Substrate"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Phosphocysteine intermediate","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bzc
ChainResidueDetails
AARG2414
AASP2378
ASER2415
ACYS2408

239149

PDB entries from 2025-07-23

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