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6NJT

Mouse endonuclease G mutant - H97A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0003676molecular_functionnucleic acid binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 301
ChainResidue
AASN128
AHOH407
AHOH429
AHOH436
AHOH522
AHOH524

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 302
ChainResidue
AHOH595
AARG72
AGLU73
AASN85

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 303
ChainResidue
AARG95
BCYS69

site_idAC4
Number of Residues5
Detailsbinding site for residue CL A 304
ChainResidue
AARG160
ALYS170
BARG144
BARG160
BLYS170

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 305
ChainResidue
AALA102
AHOH563
BGLN129

site_idAC6
Number of Residues1
Detailsbinding site for residue CL A 306
ChainResidue
ASER225

site_idAC7
Number of Residues2
Detailsbinding site for residue CL A 308
ChainResidue
AGLU19
ALEU20

site_idAC8
Number of Residues5
Detailsbinding site for residue IPA A 309
ChainResidue
AGLN172
AILE174
AGLY175
AHOH441
AHOH450

site_idAC9
Number of Residues2
Detailsbinding site for residue IPA A 310
ChainResidue
ATHR183
AASN207

site_idAD1
Number of Residues3
Detailsbinding site for residue IPA A 311
ChainResidue
AASN134
ATHR161
AGLU212

site_idAD2
Number of Residues6
Detailsbinding site for residue MG B 301
ChainResidue
BASN128
BHOH422
BHOH435
BHOH437
BHOH550
BHOH561

site_idAD3
Number of Residues3
Detailsbinding site for residue CL B 302
ChainResidue
BARG72
BGLU73
BASN85

site_idAD4
Number of Residues4
Detailsbinding site for residue CL B 303
ChainResidue
AGLN129
BALA102
BHOH532
BHOH601

site_idAD5
Number of Residues2
Detailsbinding site for residue CL B 304
ChainResidue
ACYS69
BARG95

site_idAD6
Number of Residues3
Detailsbinding site for residue CL B 305
ChainResidue
BTYR171
BGLN172
BVAL181

site_idAD7
Number of Residues4
Detailsbinding site for residue IPA B 306
ChainResidue
BSER91
BILE174
BGLY175
BHOH453

site_idAD8
Number of Residues6
Detailsbinding site for residue IPA B 307
ChainResidue
BARG66
BARG72
BARG109
BASP112
BTYR116
BHOH407

site_idAD9
Number of Residues2
Detailsbinding site for residue IPA B 308
ChainResidue
BSER225
BHOH572

site_idAE1
Number of Residues2
Detailsbinding site for residue IPA B 309
ChainResidue
BASP75
BVAL77

site_idAE2
Number of Residues7
Detailsbinding site for residue IPA B 310
ChainResidue
AILE190
APHE234
AILE238
BTYR23
BGLY24
BLEU25
BPRO26

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10047, ECO:0000269|PubMed:32095813, ECO:0000269|PubMed:32192768
ChainResidueDetails
AALA97
BALA97

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32095813, ECO:0000269|PubMed:32192768, ECO:0007744|PDB:6LYF, ECO:0007744|PDB:6NJT
ChainResidueDetails
AASN128
BASN128

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Essential for catalytic activity => ECO:0000269|PubMed:32192768
ChainResidueDetails
AARG66
BARG66

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q14249
ChainResidueDetails
ATHR84
BTHR84

220113

PDB entries from 2024-05-22

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