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4NCH

Crystal Structure of Pyrococcus furiosis Rad50 L802W 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 Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AASN32
BARG102
AGLY33
ASER34
AGLY35
ALYS36
ASER37
AHOH1014
AHOH1032
AHOH1162

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 902
ChainResidue
AVAL45
APRO50
ALEU51
AARG52
AILE53
AILE56
ALYS58
AHOH1102

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 901
ChainResidue
BTRP49
BPRO50
BLEU51
BILE53
BILE56
BLYS58

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

221371

PDB entries from 2024-06-19

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