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1SZ3

CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEXED WITH GNP AND MG+2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0005524molecular_functionATP binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 201
ChainResidue
AGLU65
AHOH765
AHOH846
AHOH853

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 202
ChainResidue
BGLU65
BHOH817
BHOH844
BHOH878

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GNP A 3030
ChainResidue
AALA15
AHIS46
ASER49
AGLY50
AALA51
AGLU69
APHE87
AASP89
AILE93
AARG95
AHOH810
AHOH845
BMET1
BGLU2
BASP4
BARG6
ALEU13

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GNP A 2030
ChainResidue
AMET1
AGLU2
AASP4
AHOH793
AHOH804
AHOH862
BLEU13
BALA15
BSER49
BGLY50
BALA51
BPHE87
BPRO88
BASP89
BVAL91
BILE93
BARG95
BHOH817
BHOH867

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 Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15123424, ECO:0007744|PDB:1SU2
ChainResidueDetails
AMET1
BARG95
AARG14
ASER49
AGLU53
AARG95
BMET1
BARG14
BSER49
BGLU53

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15123424, ECO:0007744|PDB:1SU2, ECO:0007744|PDB:1SZ3
ChainResidueDetails
AGLY50
AGLU65
APHE87
BGLY50
BGLU65
BPHE87

225946

PDB entries from 2024-10-09

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