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4YZG

Structure of the Arabidopsis TAP38/PPH1, a state-transition phosphatase responsible for dephosphorylation of LHCII

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 Residues6
Detailsbinding site for residue MN A 401
ChainResidue
AASP93
AGLY94
AHOH507
AHOH518
AHOH589
AHOH596

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 402
ChainResidue
AHOH518
AHOH531
AHOH625
AASP93
AASP296
AASP339

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG69
AHOH507
AHOH518
AHOH531
BLYS261
BARG265

site_idAC4
Number of Residues6
Detailsbinding site for residue MN B 401
ChainResidue
BASP93
BASP296
BASP339
BHOH527
BHOH530
BHOH611

site_idAC5
Number of Residues6
Detailsbinding site for residue MN B 402
ChainResidue
BASP93
BGLY94
BHOH509
BHOH530
BHOH557
BHOH573

site_idAC6
Number of Residues7
Detailsbinding site for residue SO4 B 403
ChainResidue
ALYS261
AARG265
BARG69
BHIS95
BHOH509
BHOH516
BHOH530

Functional Information from PROSITE/UniProt
site_idPS01032
Number of Residues9
DetailsPPM_1 PPM-type phosphatase domain signature. YAAVFDGHA
ChainResidueDetails
ATYR88-ALA96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:25888588, ECO:0007744|PDB:4YZG
ChainResidueDetails
AASP93
AGLY94
AASP296
AASP339
BASP93
BGLY94
BASP296
BASP339

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PDB entries from 2024-07-24

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