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1SOI

CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEX WITH SM+3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0008828molecular_functiondATP diphosphatase activity
A0016787molecular_functionhydrolase activity
A0019177molecular_functiondihydroneopterin triphosphate pyrophosphohydrolase activity
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SM A 301
ChainResidue
AGLU65
AGLU68
AHOH730
AHOH772

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SM A 302
ChainResidue
AASP147
AARG150
AHOH743
AHOH774
AHOH788

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SM A 303
ChainResidue
AGLU12
AGLY90
AHOH753

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GavedgEnpqdAAvREAcEEtG
ChainResidueDetails
AGLY50-GLY71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsMotif: {"description":"Nudix box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15123424","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15123424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SU2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15123424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SU2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SZ3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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