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3QF7

The Mre11:Rad50 complex forms an ATP dependent molecular clamp in DNA double-strand break repair

Functional Information from GO Data
ChainGOidnamespacecontents
A0006302biological_processdouble-strand break repair
A0016887molecular_functionATP hydrolysis activity
B0006302biological_processdouble-strand break repair
B0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE ANP A 853
ChainResidue
ALEU12
ASER38
AARG53
ATYR54
AASP59
AVAL61
AASN62
AARG63
AGLN142
AGLU798
AMG854
AGLY13
AHOH863
AHOH864
AHOH874
AHOH931
BARG741
BARG762
BGLY766
BSER768
BGLY769
BGLY770
APRO31
BGLU771
AASN32
AGLY33
AALA34
AGLY35
ALYS36
ASER37

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 854
ChainResidue
ASER37
AGLN142
AANP853
AHOH863
AHOH876

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ANP B 853
ChainResidue
AARG741
AARG762
AGLY766
ASER768
AGLY769
AGLY770
AGLU771
AHOH882
BLEU12
BGLY13
BPRO31
BASN32
BGLY33
BALA34
BGLY35
BLYS36
BSER37
BSER38
BARG53
BTYR54
BASP59
BVAL61
BASN62
BARG63
BGLN142
BGLU798
BMG854
BHOH855
BHOH881

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 854
ChainResidue
BSER37
BGLN142
BANP853
BHOH855
BHOH856

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGERALISISLAM
ChainResidueDetails
ALEU767-MET781

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:21458667, ECO:0007744|PDB:3QF7
ChainResidueDetails
AASN32
BASN32

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:21937514, ECO:0007744|PDB:3THO
ChainResidueDetails
AGLY33
AALA34
ATYR54
BGLY33
BALA34
BTYR54

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|PubMed:21458667, ECO:0000305|PubMed:21937514, ECO:0000305|PubMed:25349191, ECO:0007744|PDB:3QF7, ECO:0007744|PDB:3THO, ECO:0007744|PDB:4W9M
ChainResidueDetails
AGLY35
BARG63
ALYS36
ASER38
AARG53
AARG63
BGLY35
BLYS36
BSER38
BARG53

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:21458667, ECO:0000305|PubMed:25349191, ECO:0007744|PDB:3QF7, ECO:0007744|PDB:4W9M
ChainResidueDetails
ASER37
AGLN142
BSER37
BGLN142

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:21458667, ECO:0000305|PubMed:25349191, ECO:0007744|PDB:3QF7, ECO:0007744|PDB:3THO, ECO:0007744|PDB:4W9M
ChainResidueDetails
AASP59
BASP59

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:21458667, ECO:0000305|PubMed:21937514, ECO:0007744|PDB:3QF7, ECO:0007744|PDB:3THO
ChainResidueDetails
AVAL61
BVAL61

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:4W9M
ChainResidueDetails
AASP797
BASP797

222415

PDB entries from 2024-07-10

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