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6HOZ

ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with inosine diphosphate ribose (IDPr)

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
AR5I403
AR7I404
AHOH627

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
AASP305
ATHR306
AR5I403
AR7I404
AGLU33
AASP303

site_idAC3
Number of Residues29
Detailsbinding site for residue R5I A 403
ChainResidue
AGLU33
AASP63
AASP64
AGLY101
AGLY103
AALA104
AGLY105
AVAL106
APHE129
AGLY133
ASER134
ATYR135
AGLY136
AASN137
AGLY138
AHIS168
AILE260
AASP303
AASP305
ATHR306
AMG401
AMG402
AR7I404
AHOH506
AHOH514
AHOH521
AHOH575
AHOH597
BHOH620

site_idAC4
Number of Residues29
Detailsbinding site for residue R7I A 404
ChainResidue
AGLU33
AASP63
AASP64
AGLY101
AGLY103
AGLY105
AVAL106
APHE129
AGLY133
ASER134
ATYR135
AGLY136
AASN137
AGLY138
AHIS168
AILE260
AASP303
AASP305
ATHR306
AMG401
AMG402
AR5I403
AHOH506
AHOH510
AHOH514
AHOH521
AHOH575
AHOH627
BHOH620

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 405
ChainResidue
AASP80
AASP155
AGLN352
AHOH570

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
AASN152
AGLN154
AASP155
ALYS158
AHOH593
BGLN123
BARG126

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL A 407
ChainResidue
AASN175
AGLU209
APHE231

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 408
ChainResidue
AGLU337
AGLU340
BSER11
BLEU12
BALA13

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL A 409
ChainResidue
AGLU97
ATHR99
AARG100
AHOH578
BTHR99
BHOH528

site_idAD1
Number of Residues6
Detailsbinding site for residue ACT A 410
ChainResidue
APHE60
AHOH502
AHOH586
AGLU31
ATHR58
ALEU59

site_idAD2
Number of Residues7
Detailsbinding site for residue MG B 401
ChainResidue
BTHR62
BASP63
BASP64
BASP305
BR5I403
BR7I404
BHOH616

site_idAD3
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
BGLU33
BASP303
BASP305
BTHR306
BR5I403
BR7I404

site_idAD4
Number of Residues30
Detailsbinding site for residue R5I B 403
ChainResidue
AASP42
AHOH518
BGLU33
BASP63
BASP64
BGLY101
BGLY103
BGLY105
BVAL106
BPHE129
BGLY133
BSER134
BTYR135
BGLY136
BASN137
BGLY138
BHIS168
BILE260
BASP303
BASP305
BTHR306
BMG401
BMG402
BR7I404
BHOH512
BHOH526
BHOH560
BHOH567
BHOH587
BHOH644

site_idAD5
Number of Residues31
Detailsbinding site for residue R7I B 404
ChainResidue
AALA37
AHOH518
BGLU33
BASP63
BASP64
BGLY101
BGLY103
BGLY105
BVAL106
BPHE129
BGLY133
BSER134
BTYR135
BGLY136
BASN137
BGLY138
BHIS168
BILE260
BASP303
BASP305
BTHR306
BMG401
BMG402
BR5I403
BHOH512
BHOH524
BHOH526
BHOH560
BHOH567
BHOH587
BHOH644

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL B 405
ChainResidue
BSER244
BSER245
BASN246
BHIS275
BPRO281
BHOH514

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL B 406
ChainResidue
BGLY190
BGLU191
BTYR318
BTYR319
BHOH534

site_idAD8
Number of Residues4
Detailsbinding site for residue GOL B 407
ChainResidue
BASN175
BGLU209
BPHE231
BHOH627

site_idAD9
Number of Residues4
Detailsbinding site for residue GOL B 408
ChainResidue
BARG126
BGLN165
BHOH510
BHOH569

site_idAE1
Number of Residues4
Detailsbinding site for residue GOL B 409
ChainResidue
BGLU97
BARG100
BHOH527
BHOH528

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 2024-07-17

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