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4RLP

Human p70s6k1 with ruthenium-based inhibitor FL772

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 72B A 401
ChainResidue
ALEU97
AGLU173
ATYR174
ALEU175
AGLU179
AGLU222
ATHR235
AGLY98
ALYS99
AGLY100
AGLY103
AVAL105
AALA121
ALYS123
ALEU172

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
AASP193

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 404
ChainResidue
ALYS233
AARG363

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 405
ChainResidue
ALYS325

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 406
ChainResidue
AGLN211
ALYS212

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 407
ChainResidue
AARG330

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGYGKVFqVrkvtgantgki.......FAMK
ChainResidueDetails
ALEU97-LYS123

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNIML
ChainResidueDetails
AILE214-LEU226

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
AASP218

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU97
ALYS123

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:19864428, ECO:0000269|PubMed:9445476
ChainResidueDetails
ATHR252

222624

PDB entries from 2024-07-17

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