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5CZO

Structure of S. cerevisiae Hrr25:Mam1 complex, form 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN C 201
ChainResidue
CCYS114
CHIS116
CCYS119
CCYS152

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN D 201
ChainResidue
DCYS114
DHIS116
DCYS119
DCYS152

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FiHrDIKpdNFLM
ChainResidueDetails
APHE124-MET136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP128
BASP128

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE15
AARG38
BILE15
BARG38

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950
ChainResidueDetails
ASER143
BSER143

222415

PDB entries from 2024-07-10

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