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6V0T

Crystal Structure of Catalytic Subunit of Bovine Pyruvate Dehydrogenase Phosphatase 1 - Catalytic Domain

Replaces:  3N3C
Functional Information from GO Data
ChainGOidnamespacecontents
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0043169molecular_functioncation binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 501
ChainResidue
AASP73
AGLY74
AHOH601
AHOH613
AHOH685
AHOH740

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 502
ChainResidue
AHOH610
AHOH667
AHOH685
AASP73
AASP347
AASP445

site_idAC3
Number of Residues10
Detailsbinding site for residue SO4 A 503
ChainResidue
ASER290
ASER290
AILE291
AILE291
AASP292
AASP292
ASO4504
ASO4504
AMN506
AMN506

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 A 504
ChainResidue
AILE291
AASP292
AASP292
ASO4503
ASO4503
AMN507
AMN507

site_idAC5
Number of Residues3
Detailsbinding site for residue MN A 505
ChainResidue
AHIS410
AHIS414
AHOH622

site_idAC6
Number of Residues7
Detailsbinding site for residue MN A 506
ChainResidue
ASER290
AILE291
APRO321
ASO4503
ASO4503
AHOH626
AHOH779

site_idAC7
Number of Residues3
Detailsbinding site for residue MN A 507
ChainResidue
AASP292
ASO4504
ASO4504

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 Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:32627744, ECO:0000269|Ref.6, ECO:0007744|PDB:3MQ3, ECO:0007744|PDB:6V0T
ChainResidueDetails
AASP347
AASP445
AASP73
AGLY74

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9P0J1
ChainResidueDetails
ALYS131

219869

PDB entries from 2024-05-15

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