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2PNQ

Crystal structure of pyruvate dehydrogenase phosphatase 1 (PDP1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0043169molecular_functioncation binding
B0004722molecular_functionprotein serine/threonine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0043169molecular_functioncation binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AASP73
AGLY74
AHOH503
AHOH505
AHOH506

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AHOH504
AHOH507
AASP73
AASP347
AASP445
AHOH503

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 503
ChainResidue
BASP73
BGLY74
BHOH505
BHOH507
BHOH508

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 504
ChainResidue
BASP73
BASP347
BASP445
BHOH505
BHOH506
BHOH509

Functional Information from PROSITE/UniProt
site_idPS01032
Number of Residues9
DetailsPPM_1 PPM-type phosphatase domain signature. LLGVFDGHA
ChainResidueDetails
ALEU68-ALA76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17532339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PNQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9P0J1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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