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6HH5

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

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 Residues6
Detailsbinding site for residue MG A 401
ChainResidue
ATHR62
AASP63
AASP64
AASP305
AHOH518
AHOH540

site_idAC2
Number of Residues24
Detailsbinding site for residue A3R A 402
ChainResidue
AGLY103
AALA104
AGLY105
AVAL106
APHE129
AGLY133
ASER134
ATYR135
AGLY136
AASN137
AGLY138
AHIS168
AILE260
AASP303
ATHR306
AHOH518
AHOH519
AHOH533
AHOH539
AHOH548
BASP42
AGLU33
AASP63
AGLY101

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 403
ChainResidue
AASP80
AASP155
APHE159
AGLN352
AHOH511
BSER119
BHOH575

site_idAC4
Number of Residues6
Detailsbinding site for residue MG B 401
ChainResidue
BTHR62
BASP63
BASP64
BASP305
BHOH535
BHOH604

site_idAC5
Number of Residues20
Detailsbinding site for residue A3R B 402
ChainResidue
AALA37
BASP63
BGLY101
BGLY103
BALA104
BGLY105
BVAL106
BPHE129
BGLY133
BSER134
BTYR135
BGLY136
BASN137
BGLY138
BHIS168
BILE260
BHOH503
BHOH528
BHOH538
BHOH589

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL B 403
ChainResidue
BSER245
BASN246
BHIS275
BPRO281
BHOH515

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

222036

PDB entries from 2024-07-03

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