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1USH

5'-NUCLEOTIDASE FROM E. COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0009166biological_processnucleotide catabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 600
ChainResidue
AASP84
AGLN254
AZN601
ACO3602
AASP41
AHIS43

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
AASP84
AASN116
AHIS217
AHIS252
AZN600
ACO3602

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CO3 A 602
ChainResidue
AASP41
AASP84
AASN116
AHIS117
AHIS252
AGLN254
ATHR518
AGLY519
AZN600
AZN601
AHOH1189

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AARG375
AARG379
AARG410

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
ATRP47
AARG48
AHOH908
AHOH931
AHOH1147

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 605
ChainResidue
AASN342
AGLN343
AHOH628
AHOH945

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 606
ChainResidue
ALYS68
AGLY148
AARG190
AHOH862
AHOH975
AHOH1024
AHOH1183

site_idZNB
Number of Residues7
DetailsZN BINDING SITE
ChainResidue
AASP41
AHIS43
AASP84
AASN116
AHIS217
AHIS252
AGLN254

Functional Information from PROSITE/UniProt
site_idPS00785
Number of Residues13
Details5_NUCLEOTIDASE_1 5'-nucleotidase signature 1. ItVLHTnDhHGhF
ChainResidueDetails
AILE34-PHE46

site_idPS00786
Number of Residues12
Details5_NUCLEOTIDASE_2 5'-nucleotidase signature 2. YdamaIGNHEFD
ChainResidueDetails
ATYR109-ASP120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AASP41
AHIS43
AASP84
AASN116
AHIS217
AHIS252
AGLN254
AARG375
APHE498

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AHIS117
AASP120

Catalytic Information from CSA
site_idCSA1
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 10331872, 11491293
ChainResidueDetails
AARG375
AASP120
AARG410
AHIS117
AARG379
AASN116

site_idMCSA1
Number of Residues12
DetailsM-CSA 611
ChainResidueDetails
AASP41metal ligand
AARG375electrostatic stabiliser, increase acidity, increase electrophilicity
AARG379electrostatic stabiliser, increase acidity, increase electrophilicity
AARG410electrostatic stabiliser, increase acidity, increase electrophilicity
AHIS43metal ligand
AASP84metal ligand
AASN116electrostatic stabiliser, metal ligand
AHIS117electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor
AASP120electrostatic stabiliser, increase basicity
AHIS217metal ligand
AHIS252metal ligand
AGLN254metal ligand

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PDB entries from 2024-09-11

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