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3H62

Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with cantharidic acid

Functional Information from GO Data
ChainGOidnamespacecontents
B0016787molecular_functionhydrolase activity
C0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 500
ChainResidue
CNHC0
CASP271
CASN303
CHIS352
CHIS427
CMN501

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 501
ChainResidue
CASP271
CMN500
CNHC0
CASP242
CHIS244

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NHC C 0
ChainResidue
CASP242
CHIS244
CASP271
CARG275
CASN303
CHIS304
CARG400
CHIS427
CVAL429
CPHE446
CTYR451
CMN500
CMN501

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 500
ChainResidue
BNHC0
BASP271
BASN303
BHIS352
BHIS427
BMN501

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 501
ChainResidue
BNHC0
BASP242
BHIS244
BASP271
BMN500

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NHC B 0
ChainResidue
BASP242
BHIS244
BASP271
BARG275
BASN303
BHIS304
BARG400
BHIS427
BVAL429
BPHE446
BTYR451
BMN500
BMN501
BHOH690

Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
CLEU300-GLU305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:15155720
ChainResidueDetails
CHIS304
BHIS304

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64
ChainResidueDetails
CASP242
CASP271
CASN303
CHIS352
BASP242
BASP271
BASN303
BHIS352

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15155720
ChainResidueDetails
CHIS244
CARG275
CARG400
CHIS427
BHIS244
BARG275
BARG400
BHIS427

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
CHIS304
CASP274

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
BHIS304
BASP274

site_idMCSA1
Number of Residues10
DetailsM-CSA 472
ChainResidueDetails
CASP242metal ligand
CHIS427activator, metal ligand
CHIS244metal ligand
CASP271metal ligand
CASP274activator, proton donor
CARG275transition state stabiliser
CASN303metal ligand, transition state stabiliser
CHIS304proton acceptor, proton donor, proton relay
CHIS352metal ligand
CARG400transition state stabiliser

site_idMCSA2
Number of Residues10
DetailsM-CSA 472
ChainResidueDetails
BASP242metal ligand
BHIS427activator, metal ligand
BHIS244metal ligand
BASP271metal ligand
BASP274activator, proton donor
BARG275transition state stabiliser
BASN303metal ligand, transition state stabiliser
BHIS304proton acceptor, proton donor, proton relay
BHIS352metal ligand
BARG400transition state stabiliser

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PDB entries from 2024-07-24

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