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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: BINDING => ECO:0000269|PubMed:17532339, ECO:0007744|PDB:2PNQ
ChainResidueDetails
AASP73
AGLY74
AASP347
AASP445
BASP73
BGLY74
BASP347
BASP445

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9P0J1
ChainResidueDetails
ALYS131
BLYS131

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PDB entries from 2024-07-24

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