Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4NV0

Crystal structure of cytosolic 5'-nucleotidase IIIB (cN-IIIB) bound to 7-methylguanosine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008252molecular_functionnucleotidase activity
A0008253molecular_function5'-nucleotidase activity
A0009117biological_processnucleotide metabolic process
A0009158biological_processribonucleoside monophosphate catabolic process
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0106411molecular_functionXMP 5'-nucleosidase activity
A1901069biological_processguanosine-containing compound catabolic process
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008252molecular_functionnucleotidase activity
B0008253molecular_function5'-nucleotidase activity
B0009117biological_processnucleotide metabolic process
B0009158biological_processribonucleoside monophosphate catabolic process
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0106411molecular_functionXMP 5'-nucleosidase activity
B1901069biological_processguanosine-containing compound catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PGE A 401
ChainResidue
AARG13
BHOH695
AALA33
AGLU36
AARG37
AASN40
AILE44
AHOH723
AHOH768
BGLU155

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AASP55
AASP57
AASP245
AMGF404
AHOH626
AHOH627

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MG7 A 403
ChainResidue
AASP57
APHE75
AARG100
AGLU103
ATRP120
ATRP121
ASER124
AGLY173
AHOH515
AHOH540
AHOH579
AHOH586
AHOH605
AHOH662
AHOH776

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MGF A 404
ChainResidue
AASP55
APHE56
AASP57
ASER171
AALA172
ALYS219
AMG402
AHOH523
AHOH540
AHOH626
AHOH627

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP55
BASP57
BASP245
BMGF403
BHOH644
BHOH645

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE MG7 B 402
ChainResidue
BSER73
BPHE75
BASN79
BTYR96
BGLU103
BTRP120
BTRP121
BSER124
BHOH502
BHOH521
BHOH554
BHOH574
BHOH639
BHOH663
BHOH693
BHOH719

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MGF B 403
ChainResidue
BASP55
BPHE56
BASP57
BSER171
BALA172
BLYS219
BMG401
BHOH502
BHOH506
BHOH644
BHOH645

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:24603684
ChainResidueDetails
AASP55
BASP55

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:24603684
ChainResidueDetails
AASP57
BASP57

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:24603684
ChainResidueDetails
AASP245
BASP55
BASP57
BGLU103
BSER124
BASP245
AASP55
AASP57
AGLU103
ASER124

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9H0P0
ChainResidueDetails
ASER171
BSER171

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon