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5XZV

Crystal structure of Rad53 1-466 in complex with AMP-PNP

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 Residues12
Detailsbinding site for residue ANP A 501
ChainResidue
AGLY205
AVAL276
AASP280
AASP339
APHE209
AALA210
AVAL212
AALA225
ALYS227
AILE229
AGLU244
AGLU274

site_idAC2
Number of Residues8
Detailsbinding site for residue ANP B 501
ChainResidue
BGLY205
BALA225
BGLU274
BPHE275
BVAL276
BASP280
BASP323
BLEU326

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGQGAFATVKkAierttgkt..........FAVK
ChainResidueDetails
AVAL204-LYS227

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IsHrDLKpdNILI
ChainResidueDetails
AILE315-ILE327

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP319
BASP319

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL204
ALYS227
BVAL204
BLYS227

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER24
ASER175
BSER24
BSER175

218853

PDB entries from 2024-04-24

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