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3QKU

Mre11 Rad50 binding domain in complex with Rad50 and AMP-PNP

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 Residues24
DetailsBINDING SITE FOR RESIDUE ANP A 1001
ChainResidue
AARG12
ASER38
AGLU60
ATHR62
ALYS63
AVAL64
AGLN140
ALYS763
ATYR764
APHE791
ASER793
ASER13
AGLY794
AGLY795
AGLU796
AGLU823
AMG1002
AGLN31
AASN32
AGLY33
ASER34
AGLY35
ALYS36
ASER37

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1002
ChainResidue
ASER37
AGLN140
AASP822
AANP1001

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ANP B 1001
ChainResidue
BARG12
BSER13
BGLN31
BASN32
BGLY33
BSER34
BGLY35
BLYS36
BSER37
BSER38
BGLU60
BTHR62
BLYS63
BVAL64
BGLN140
BLYS763
BTYR764
BPHE791
BSER793
BGLY794
BGLY795
BGLU796
BGLU823
BMG1002

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1002
ChainResidue
BSER37
BGLN140
BASP822
BGLU823
BANP1001

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0000269|PubMed:24493214, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT, ECO:0007744|PDB:3QKU, ECO:0007744|PDB:4NCJ
ChainResidueDetails
AARG12
AASN32
AGLU60
BARG12
BASN32
BGLU60

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT, ECO:0007744|PDB:3QKU
ChainResidueDetails
AGLN140
BGLN140

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT
ChainResidueDetails
ALYS763
APHE791
BLYS763
BPHE791

218853

PDB entries from 2024-04-24

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