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4MOY

Structure of a second nuclear PP1 Holoenzyme, crystal form 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AASP64
AHIS66
AASP92
AMN402
APO4404
AHOH633
AHOH634

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AHIS173
AHIS248
AMN401
APO4404
AHOH634
AASP92
AASN124

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
AGLY215
AGLY228
AALA229
AGLU230
AVAL231

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PO4 A 404
ChainResidue
AHIS66
AASP92
AARG96
AASN124
AHIS125
AARG221
AHIS248
AMN401
AMN402
AHOH633
AHOH634

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
APRO50
AGLU54
AGLU116
APHE119

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
ACYS127
ASER129
AVAL195
AHOH538

Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU121-GLU126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:12574161
ChainResidueDetails
BTHR398

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP64
AHIS66

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP92
AASN124
AHIS173
AHIS248

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER22

221051

PDB entries from 2024-06-12

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