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2A8T

2.1 Angstrom Crystal Structure of the Complex Between the Nuclear U8 snoRNA Decapping Nudix Hydrolase X29, Manganese and m7G-PPP-A

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
A0035863biological_processdITP catabolic process
A0035870molecular_functiondITP diphosphatase activity
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
A0090068biological_processpositive regulation of cell cycle process
A0097383molecular_functiondIDP phosphatase activity
A0110152molecular_functionRNA NAD+-cap (NAD+-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
B0035863biological_processdITP catabolic process
B0035870molecular_functiondITP diphosphatase activity
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
B0090068biological_processpositive regulation of cell cycle process
B0097383molecular_functiondIDP phosphatase activity
B0110152molecular_functionRNA NAD+-cap (NAD+-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 Residues5
DetailsBINDING SITE FOR RESIDUE MN A 300
ChainResidue
AGLY72
AGLU93
AMGT251
AMN301
AHOH633

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 301
ChainResidue
AMN300
AMN303
AHOH505
AGLU89
AGLU93
AGLU150
AMGT251

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 302
ChainResidue
AARG88
AGLU89
AMGT251
AMN303

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 303
ChainResidue
AGLU150
AMGT251
AMN301
AMN302

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 304
ChainResidue
BGLY72
BGLU93
BMGT251
BMN305
BHOH635

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MN B 305
ChainResidue
BGLY72
BGLU89
BGLU92
BGLU93
BASP146
BGLU150
BMGT251
BMN304
BMN306

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 306
ChainResidue
BGLU89
BGLU150
BMGT251
BMN305
BHOH615
BHOH628
BHOH629

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MGT A 251
ChainResidue
AHIS37
AARG63
APHE64
AGLY72
AGLY73
APHE74
AGLU89
AGLU93
AGLU150
AADN252
AMN300
AMN301
AMN302
AMN303
BPHE49

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ADN A 252
ChainResidue
AHIS37
APHE74
ATHR122
AILE178
AASN180
ASER181
AGLN184
AMGT251
AHOH639

site_idBC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MGT B 251
ChainResidue
APHE49
BHIS37
BARG63
BPHE64
BGLY72
BGLY73
BPHE74
BGLU89
BGLU93
BGLU150
BADN252
BMN304
BMN305
BMN306
BHOH635

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ADN B 252
ChainResidue
BHIS37
BPHE70
BPHE74
BTHR122
BILE178
BASN180
BSER181
BGLN184
BMGT251

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:16472752
ChainResidueDetails
AHIS37
BARG63
BGLY72
BGLU89
BGLU93
BGLU150
BASN180
BGLN184
AARG63
AGLY72
AGLU89
AGLU93
AGLU150
AASN180
AGLN184
BHIS37

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q96DE0
ChainResidueDetails
APHE70
BPHE70

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PDB entries from 2024-11-06

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