Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5F3W

Structure of the ATPrS-Mre11/Rad50-DNA complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000403molecular_functionY-form DNA binding
A0003677molecular_functionDNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004527molecular_functionexonuclease activity
A0004529molecular_functionDNA exonuclease activity
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0006974biological_processDNA damage response
A0008408molecular_function3'-5' exonuclease activity
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0042802molecular_functionidentical protein binding
A0045027molecular_functionDNA end binding
A0046872molecular_functionmetal ion binding
B0006302biological_processdouble-strand break repair
B0016887molecular_functionATP hydrolysis activity
C0000403molecular_functionY-form DNA binding
C0003677molecular_functionDNA binding
C0004518molecular_functionnuclease activity
C0004519molecular_functionendonuclease activity
C0004527molecular_functionexonuclease activity
C0004529molecular_functionDNA exonuclease activity
C0006281biological_processDNA repair
C0006302biological_processdouble-strand break repair
C0006974biological_processDNA damage response
C0008408molecular_function3'-5' exonuclease activity
C0016787molecular_functionhydrolase activity
C0030145molecular_functionmanganese ion binding
C0042802molecular_functionidentical protein binding
C0045027molecular_functionDNA end binding
C0046872molecular_functionmetal ion binding
D0006302biological_processdouble-strand break repair
D0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 401
ChainResidue
AASP8
AHIS10
AASP49
AHIS188
AMG402

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 402
ChainResidue
AMG401
AASP49
AASN84
AHIS158
AHIS186

site_idAC3
Number of Residues22
Detailsbinding site for residue AGS B 1101
ChainResidue
BLYS14
BSER15
BGLY35
BSER36
BGLY37
BLYS38
BSER39
BSER40
BTHR60
BILE62
BTHR63
BLYS64
BGLN134
BASP946
BGLU947
BLYS994
DTYR890
DLEU910
DASN914
DSER916
DGLY917
DGLU919

site_idAC4
Number of Residues5
Detailsbinding site for residue MG C 401
ChainResidue
CASP49
CASN84
CHIS158
CHIS186
CMG402

site_idAC5
Number of Residues5
Detailsbinding site for residue MG C 402
ChainResidue
CASP8
CHIS10
CASP49
CHIS188
CMG401

site_idAC6
Number of Residues21
Detailsbinding site for residue AGS D 1101
ChainResidue
BTYR890
BLEU910
BASN914
BSER916
BGLU919
DLYS14
DSER15
DGLU33
DGLY35
DSER36
DGLY37
DLYS38
DSER39
DSER40
DTHR60
DILE62
DTHR63
DLYS64
DGLN134
DGLU947
DLYS994

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_02044","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02044","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00449","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3AUY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3AUX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AUY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00449","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon