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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
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues50
DetailsDomain: {"description":"FHA 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00086","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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