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1S95

Structure of serine/threonine protein phosphatase 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 501
ChainResidue
AASP242
AHIS244
AASP271
AMN502
APO41001
AHOH3002
AHOH3003

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 502
ChainResidue
AHIS352
AHIS427
AMN501
APO41001
AHOH3002
AASP271
AASN303

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 601
ChainResidue
BASP242
BHIS244
BASP271
BMN602
BPO42001
BHOH3003
BHOH3004

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 602
ChainResidue
BASP271
BASN303
BHIS352
BHIS427
BMN601
BPO42001
BHOH3003

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PO4 A 1001
ChainResidue
AHIS244
AASP271
AARG275
AASN303
AHIS304
AARG400
AHIS427
AMN501
AMN502
AHOH3002
AHOH3003
AHOH3175
AHOH3182
BMET499

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 B 2001
ChainResidue
BHIS244
BASP271
BARG275
BASN303
BHIS304
BARG400
BHIS427
BMN601
BMN602
BHOH3003
BHOH3004
BHOH3087

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 3001
ChainResidue
ALYS192
ALEU251
AGLU255

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 3002
ChainResidue
BLYS192
BGLN196
BGLU255

Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU300-GLU305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:15155720
ChainResidueDetails
AHIS304
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
AASP242
AASP271
AASN303
AHIS352
BASP242
BASP271
BASN303
BHIS352

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15155720
ChainResidueDetails
AHIS244
AARG275
AARG400
AHIS427
BHIS244
BARG275
BARG400
BHIS427

Catalytic Information from CSA
site_idCSA1
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 15155720
ChainResidueDetails
AHIS304
AASP274
AARG400
AARG275
AASN303
AHIS427

site_idCSA2
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 15155720
ChainResidueDetails
BHIS304
BASP274
BARG400
BARG275
BASN303
BHIS427

site_idMCSA1
Number of Residues10
DetailsM-CSA 472
ChainResidueDetails
AASP242metal ligand
AHIS427activator, metal ligand
AHIS244metal ligand
AASP271metal ligand
AASP274activator, proton donor
AARG275transition state stabiliser
AASN303metal ligand, transition state stabiliser
AHIS304proton acceptor, proton donor, proton relay
AHIS352metal ligand
AARG400transition 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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