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4NCK

Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 901
ChainResidue
BPRO50
BLEU51
BARG52
BILE53
BILE56
BLYS57
BLYS58

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 902
ChainResidue
BSER37
BGLY35
BLYS36

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 903
ChainResidue
BGLU758

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

225158

數據於2024-09-18公開中

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