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6G1Q

ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with ADP-ribose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004649molecular_functionpoly(ADP-ribose) glycohydrolase activity
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006281biological_processDNA repair
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0060546biological_processnegative regulation of necroptotic process
A0140290biological_processpeptidyl-serine ADP-deribosylation
B0000287molecular_functionmagnesium ion binding
B0004649molecular_functionpoly(ADP-ribose) glycohydrolase activity
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006281biological_processDNA repair
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0060546biological_processnegative regulation of necroptotic process
B0140290biological_processpeptidyl-serine ADP-deribosylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MG A 401
ChainResidue
ATHR62
AASP63
AASP64
AASP305
AAR6402
AHOH501
AHOH519

site_idAC2
Number of Residues26
Detailsbinding site for residue AR6 A 402
ChainResidue
AASP64
AGLY101
AGLY103
AALA104
AGLY105
AVAL106
APHE129
AGLY133
ASER134
ATYR135
AGLY136
AASN137
AGLY138
AHIS168
AILE260
AASP303
AASP305
ATHR306
AMG401
AHOH501
AHOH503
AHOH509
BALA37
BASP42
AGLU33
AASP63

site_idAC3
Number of Residues6
Detailsbinding site for residue MG B 401
ChainResidue
BTHR62
BASP63
BASP64
BASP305
BAR6402
BHOH525

site_idAC4
Number of Residues24
Detailsbinding site for residue AR6 B 402
ChainResidue
AASP42
BGLU33
BASP63
BASP64
BGLY101
BGLY103
BALA104
BGLY105
BVAL106
BPHE129
BGLY133
BSER134
BTYR135
BGLY136
BASN137
BGLY138
BHIS168
BILE260
BASP303
BASP305
BTHR306
BMG401
BHOH501
BHOH525

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7AQM
ChainResidueDetails
AASP26
BASP26

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:30472116, ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7AQM
ChainResidueDetails
AGLU33
AASP64
AASP303
AASP305
BGLU33
BASP64
BASP303
BASP305

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:30472116
ChainResidueDetails
ATHR62
BHIS168
BILE260
BTHR306
AASP63
ALYS132
AHIS168
AILE260
ATHR306
BTHR62
BASP63
BLYS132

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Glutamate flap => ECO:0000250|UniProtKB:Q9NX46
ChainResidueDetails
AGLU33
BGLU33

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PDB entries from 2024-05-01

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