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6G1P

Apo form of ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae

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
AHOH523
AHOH742

site_idAC2
Number of Residues15
Detailsbinding site for residue CIT A 402
ChainResidue
AGLY103
AALA104
AGLY136
AASN137
AGLY138
AMET141
AHIS168
AILE260
AHOH508
AHOH521
AHOH547
BGLU33
AASP63
AGLY101
ATYR102

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 403
ChainResidue
ATYR118
ASER119
AASP120
AHOH545
AHOH776

site_idAC4
Number of Residues5
Detailsbinding site for residue ACT A 404
ChainResidue
AGLU51
ALEU286
AGLN291
AHOH512
AHOH567

site_idAC5
Number of Residues2
Detailsbinding site for residue ACT A 405
ChainResidue
AARG48
ALYS52

site_idAC6
Number of Residues5
Detailsbinding site for residue ACT A 406
ChainResidue
AMET9
AGLN14
ALEU188
AGLN189
AHOH728

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL A 407
ChainResidue
AGLU191
ATYR318
ATYR319

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 408
ChainResidue
AALA37
AVAL38
ASER299
ALEU300
AGLY301
AHOH504

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL A 409
ChainResidue
AGLN108
ALYS111
BGLU31
BPHE46
BLEU49
BLEU50
BTHR58

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL A 410
ChainResidue
AASP80
AASP155
APHE159
AGLN352
AHOH529

site_idAD2
Number of Residues6
Detailsbinding site for residue MG B 401
ChainResidue
BTHR62
BASP63
BASP64
BASP305
BHOH554
BHOH735

site_idAD3
Number of Residues15
Detailsbinding site for residue CIT B 402
ChainResidue
AGLU33
BASP63
BGLY101
BTYR102
BGLY103
BALA104
BGLY136
BASN137
BGLY138
BMET141
BHIS168
BILE260
BHOH505
BHOH518
BHOH548

site_idAD4
Number of Residues4
Detailsbinding site for residue ACT B 403
ChainResidue
BPHE122
BARG126
BGLN165
BHOH704

site_idAD5
Number of Residues5
Detailsbinding site for residue ACT B 404
ChainResidue
BGLU51
BLEU286
BGLN291
BHOH527
BHOH597

site_idAD6
Number of Residues3
Detailsbinding site for residue ACT B 405
ChainResidue
BASN288
BASP322
BHOH726

site_idAD7
Number of Residues8
Detailsbinding site for residue GOL B 406
ChainResidue
BHOH713
BALA37
BVAL38
BALA250
BSER299
BLEU300
BGLY301
BHOH502

site_idAD8
Number of Residues9
Detailsbinding site for residue GOL B 407
ChainResidue
ASER35
AASP36
AHOH522
BPHE129
BSER134
BTYR135
BGLY136
BILE260
BALA261

site_idAD9
Number of Residues8
Detailsbinding site for residue GOL B 408
ChainResidue
AGLU31
APHE46
ALEU49
ALEU50
ATHR58
BGLN108
BLYS111
BHOH637

site_idAE1
Number of Residues6
Detailsbinding site for residue GOL B 409
ChainResidue
BARG126
BGLY131
BLYS132
BGLY133
BALA169
BHOH564

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
BASP303
BASP305
AGLU33
AASP64
AASP303
AASP305
BGLU33
BASP64

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

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

221051

PDB entries from 2024-06-12

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