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1D1Q

CRYSTAL STRUCTURE OF A YEAST LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE (LTP1) COMPLEXED WITH THE SUBSTRATE PNPP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003993molecular_functionacid phosphatase activity
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006470biological_processprotein dephosphorylation
A0016787molecular_functionhydrolase activity
B0003993molecular_functionacid phosphatase activity
B0004721molecular_functionphosphoprotein phosphatase activity
B0004725molecular_functionprotein tyrosine phosphatase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006470biological_processprotein dephosphorylation
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 402
ChainResidue
BALA13
BHOH426
BLEU14
BGLY15
BASN16
BPHE17
BCYS18
BARG19
BSER20
BHOH415

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 4NP A 401
ChainResidue
AGLU3
AALA13
ALEU14
AGLY15
AASN16
APHE17
ACYS18
AARG19
AASP132
ATRP134
AHOH457
BTYR51
BHOH432

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
AILE64
AGLN67
AGLN139
AHOH436
AHOH469
AHOH490
AHOH491
BTRP134
BTYR135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10684639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D1Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"10684639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D1Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10684639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D1Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"10684639","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D1Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10684639, 12882518, 10409830
ChainResidueDetails
AALA13
AARG19
ASER20
AASP132

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10684639, 12882518, 10409830
ChainResidueDetails
BALA13
BARG19
BSER20
BASP132

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PDB entries from 2025-10-08

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