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6HH4

ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with ADP-ribosyl-L-arginine

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
AF2R403
AHOH679

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 402
ChainResidue
ATHR306
AF2R403
AGLU33
AASP303
AASP305

site_idAC3
Number of Residues33
Detailsbinding site for residue F2R A 403
ChainResidue
AGLU33
AASP63
AASP64
AGLY101
ATYR102
AGLY103
AGLY105
AVAL106
APHE129
AGLY133
ASER134
ATYR135
AGLY136
AASN137
AGLY138
AHIS168
AILE260
AASP303
AASP305
ATHR306
AMG401
AMG402
AHOH508
AHOH519
AHOH542
AHOH565
AHOH573
AHOH584
AHOH606
AHOH644
AHOH692
BALA30
BGLU31

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 404
ChainResidue
APRO79
AASP80
AASP155
APHE159
AGLN352
AGOL405
AHOH556

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL A 405
ChainResidue
AASN152
AGLN154
AASP155
ALYS158
AGOL404
AHOH535
AHOH553
BGLN123
BARG126

site_idAC6
Number of Residues5
Detailsbinding site for residue ACT A 406
ChainResidue
AGLU51
ALEU286
AGLN291
AHOH591
AHOH602

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 401
ChainResidue
BTHR62
BASP63
BASP64
BASP305
BF2R403
BHOH670

site_idAC8
Number of Residues5
Detailsbinding site for residue MG B 402
ChainResidue
BGLU33
BASP303
BASP305
BTHR306
BF2R403

site_idAC9
Number of Residues32
Detailsbinding site for residue F2R B 403
ChainResidue
BTHR306
BMG401
BMG402
BHOH503
BHOH545
BHOH569
BHOH595
BHOH628
BHOH675
AALA30
AHOH531
AHOH532
AHOH667
BGLU33
BASP63
BASP64
BGLY101
BTYR102
BGLY103
BGLY105
BVAL106
BPHE129
BGLY133
BSER134
BTYR135
BGLY136
BASN137
BGLY138
BHIS168
BILE260
BASP303
BASP305

site_idAD1
Number of Residues3
Detailsbinding site for residue ACT B 404
ChainResidue
BGLU51
BGLN291
BHOH611

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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