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4XHL

Structure of S. cerevisiae Hrr25 1-394 (K38R mutant)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue CKI A 401
ChainResidue
AILE15
AILE23
AALA36
AASP83
ALEU85
APRO87
ASER88
AASP91
ALEU135

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 402
ChainResidue
AARG178
AGLN214
AGLY215
ALYS224

site_idAC3
Number of Residues2
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG127
ALYS154

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 404
ChainResidue
ALEU110
AGLN111
ACYS114
AARG115
ASO4406

site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 A 405
ChainResidue
AARG271
AASP275

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 406
ChainResidue
AALA270
ALYS274
AASN284
ASO4404

site_idAC7
Number of Residues1
Detailsbinding site for residue SO4 A 407
ChainResidue
AHIS347

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 A 408
ChainResidue
AARG157
AHIS162
AARG192

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP128

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE15
AARG38

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950
ChainResidueDetails
ASER143

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PDB entries from 2024-10-09

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