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5W6X

Crystal structure of the HsNUDT16 in complex with Mg+2 and ADP-ribose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0006402biological_processmRNA catabolic process
A0008235molecular_functionmetalloexopeptidase activity
A0009117biological_processnucleotide metabolic process
A0016077biological_processsno(s)RNA catabolic process
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0030515molecular_functionsnoRNA binding
A0031404molecular_functionchloride ion binding
A0035863biological_processdITP catabolic process
A0035870molecular_functiondITP diphosphatase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
A0090068biological_processpositive regulation of cell cycle process
A0097383molecular_functiondIDP phosphatase activity
A0110153molecular_functionRNA NAD-cap (NMN-forming) hydrolase activity
A0110155biological_processNAD-cap decapping
A0140933molecular_function5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity
A1990003molecular_functionIDP phosphatase activity
A1990174molecular_functionphosphodiesterase decapping endonuclease activity
A2000233biological_processnegative regulation of rRNA processing
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0003729molecular_functionmRNA binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0006402biological_processmRNA catabolic process
B0008235molecular_functionmetalloexopeptidase activity
B0009117biological_processnucleotide metabolic process
B0016077biological_processsno(s)RNA catabolic process
B0016787molecular_functionhydrolase activity
B0030145molecular_functionmanganese ion binding
B0030515molecular_functionsnoRNA binding
B0031404molecular_functionchloride ion binding
B0035863biological_processdITP catabolic process
B0035870molecular_functiondITP diphosphatase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
B0090068biological_processpositive regulation of cell cycle process
B0097383molecular_functiondIDP phosphatase activity
B0110153molecular_functionRNA NAD-cap (NMN-forming) hydrolase activity
B0110155biological_processNAD-cap decapping
B0140933molecular_function5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity
B1990003molecular_functionIDP phosphatase activity
B1990174molecular_functionphosphodiesterase decapping endonuclease activity
B2000233biological_processnegative regulation of rRNA processing
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue APR A 401
ChainResidue
AVAL22
AGLU136
AILE164
ASER166
AALA167
AGLN170
AMG402
AMG403
AHOH501
AHOH506
AHOH521
AHIS24
AHOH526
AHOH545
AHOH608
AHOH609
AHOH613
BPHE36
AARG50
AGLY59
AGLY60
APHE61
AGLU76
AGLU80
AALA108

site_idAC2
Number of Residues7
Detailsbinding site for residue MG A 402
ChainResidue
AGLU76
AGLU80
AGLU136
AAPR401
AMG403
AHOH549
AHOH562

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 403
ChainResidue
AGLY59
AGLU80
AAPR401
AMG402
AHOH605
AHOH613

site_idAC4
Number of Residues1
Detailsbinding site for residue ACY A 404
ChainResidue
ALEU13

site_idAC5
Number of Residues16
Detailsbinding site for residue APR B 401
ChainResidue
BHIS24
BARG50
BPHE51
BGLY60
BPHE61
BGLU76
BGLU80
BALA108
BGLU136
BILE164
BSER166
BGLN170
BMG402
BMG403
BHOH549
BHOH587

site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
BGLU76
BGLU80
BASP132
BGLU136
BAPR401
BHOH553

site_idAC7
Number of Residues4
Detailsbinding site for residue MG B 403
ChainResidue
BGLY59
BGLU80
BAPR401
BHOH587

site_idAC8
Number of Residues6
Detailsbinding site for residue ACY B 404
ChainResidue
BGLY82
BGLU83
BALA84
BGLY126
BARG129
BHOH511

site_idAC9
Number of Residues9
Detailsbinding site for residue PEG B 405
ChainResidue
BPRO30
BARG114
BLEU115
BTHR116
BLEU117
BHOH506
BHOH533
BHOH539
BHOH583

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:26121039
ChainResidueDetails
AHIS24
AARG50
APHE57
AGLN170
BHIS24
BARG50
BPHE57
BGLN170

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32432673, ECO:0000305|PubMed:26121039, ECO:0007744|PDB:6X7U
ChainResidueDetails
AGLY59
BGLY59

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q6TEC1
ChainResidueDetails
AGLU76
AGLU80
BGLU76
BGLU80

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:32432673, ECO:0007744|PDB:6X7U, ECO:0007744|PDB:6X7V
ChainResidueDetails
AHIS99
AGLU173
BHIS99
BGLU173

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PDB entries from 2024-04-24

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