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3RE4

Crystal Structure of Archaeoglobus Fulgidus Rio1 Kinase bound to Toyocamycin.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006468biological_processprotein phosphorylation
A0016787molecular_functionhydrolase activity
A0030490biological_processmaturation of SSU-rRNA
A0030688cellular_componentpreribosome, small subunit precursor
A0046872molecular_functionmetal ion binding
A0106310molecular_functionprotein serine kinase activity
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006468biological_processprotein phosphorylation
B0016787molecular_functionhydrolase activity
B0030490biological_processmaturation of SSU-rRNA
B0030688cellular_componentpreribosome, small subunit precursor
B0046872molecular_functionmetal ion binding
B0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE TO1 A 259
ChainResidue
AILE55
ATHR159
AILE211
AASP212
AHOH263
AHOH275
AHOH279
AHOH342
ASER56
AALA78
APRO135
AMET147
AGLU148
APHE149
AILE150
APRO156

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TO1 B 259
ChainResidue
BILE55
BSER56
BALA78
BPRO135
BMET147
BGLU148
BPHE149
BILE150
BPRO156
BILE211
BASP212
BHOH268
BHOH279
BHOH295
BHOH298

Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHaDLSEYNIMY
ChainResidueDetails
ALEU192-TYR204

site_idPS01245
Number of Residues12
DetailsRIO1 RIO1/ZK632.3/MJ0444 family signature. LVHADLSEYNiM
ChainResidueDetails
ALEU192-MET203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9BRS2, ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP196
BASP196

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250|UniProtKB:Q9BRS2
ChainResidueDetails
BASP212
AASP212

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE55
AILE55

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:16008568, ECO:0007744|PDB:1ZP9
ChainResidueDetails
ALYS80
BLYS80

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16008568, ECO:0007744|PDB:1ZP9
ChainResidueDetails
BGLU148
BILE150
AGLU148
AILE150

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O30245
ChainResidueDetails
ATYR200
BTYR200

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:16008568
ChainResidueDetails
AASP212
BASN201
BASP212
AASN201

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16008568
ChainResidueDetails
BSER108
ASER108

219869

PDB entries from 2024-05-15

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