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6X7U

Crystal Structure of the Human Nudix Hydrolase Nudt16 in complex with FAD

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
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003723molecular_functionRNA binding
C0003729molecular_functionmRNA binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0006402biological_processmRNA catabolic process
C0008235molecular_functionmetalloexopeptidase activity
C0009117biological_processnucleotide metabolic process
C0016077biological_processsno(s)RNA catabolic process
C0016787molecular_functionhydrolase activity
C0030145molecular_functionmanganese ion binding
C0030515molecular_functionsnoRNA binding
C0031404molecular_functionchloride ion binding
C0035863biological_processdITP catabolic process
C0035870molecular_functiondITP diphosphatase activity
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0050897molecular_functioncobalt ion binding
C0090068biological_processpositive regulation of cell cycle process
C0097383molecular_functiondIDP phosphatase activity
C0110153molecular_functionRNA NAD-cap (NMN-forming) hydrolase activity
C0110155biological_processNAD-cap decapping
C0140933molecular_function5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity
C1990003molecular_functionIDP phosphatase activity
C1990174molecular_functionphosphodiesterase decapping endonuclease activity
C2000233biological_processnegative regulation of rRNA processing
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue FAD A 201
ChainResidue
AALA22
AALA86
AALA87
APHE88
AVAL106
AILE164
AALA167
AGLN170
AMN202
AMN203
AHOH301
AHIS24
AHOH304
AHOH312
CPHE36
CARG38
CLEU148
AARG50
APHE51
AGLY56
APHE57
AGLY59
AGLY60
APHE61

site_idAC2
Number of Residues3
Detailsbinding site for residue MN A 202
ChainResidue
AGLY59
AGLU80
AFAD201

site_idAC3
Number of Residues2
Detailsbinding site for residue MN A 203
ChainResidue
AGLU76
AFAD201

site_idAC4
Number of Residues4
Detailsbinding site for residue MN A 204
ChainResidue
AHIS99
AGLU173
CHIS99
CGLU173

site_idAC5
Number of Residues11
Detailsbinding site for residue AMP C 201
ChainResidue
CHIS24
CARG50
CGLY56
CPHE57
CGLY59
CGLY60
CPHE61
CILE164
CGLN170
CMN202
CHOH301

site_idAC6
Number of Residues4
Detailsbinding site for residue MN C 202
ChainResidue
CGLY59
CGLY60
CGLU80
CAMP201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:26121039
ChainResidueDetails
AHIS24
AARG50
APHE57
AGLN170
CHIS24
CARG50
CPHE57
CGLN170

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32432673, ECO:0000305|PubMed:26121039, ECO:0007744|PDB:6X7U
ChainResidueDetails
AGLY59
CGLY59

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q6TEC1
ChainResidueDetails
AGLU76
AGLU80
CGLU76
CGLU80

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:32432673, ECO:0007744|PDB:6X7U, ECO:0007744|PDB:6X7V
ChainResidueDetails
AHIS99
AGLU173
CHIS99
CGLU173

224572

PDB entries from 2024-09-04

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