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1SU2

CRYSTAL STRUCTURE OF THE NUDIX HYDROLASE DR1025 IN COMPLEX WITH ATP

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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 201
ChainResidue
ALEU13
AARG14
AALA51
AATP357
AHOH720

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 202
ChainResidue
BATP257
AMET1
BSER49
BGLY50
BARG95

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 203
ChainResidue
BLEU13
BARG14
BALA51
BATP257
BHOH713

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 204
ChainResidue
ASER49
AGLY50
AARG95
AATP357
BMET1

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 205
ChainResidue
AGLU65
AHOH771
AHOH816
AHOH827
AHOH889

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 206
ChainResidue
BGLU65
BHOH764
BHOH782
BHOH853
BHOH871
BHOH980

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP B 257
ChainResidue
AMET1
AGLU2
AASP4
AARG6
BLEU13
BALA15
BGLY50
BALA51
BPHE87
BASP89
BVAL91
BILE93
BMG202
BMG203
BHOH791

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP A 357
ChainResidue
ALEU13
AALA15
AALA51
APHE87
AASP89
AVAL91
AILE93
AARG95
AMG201
AMG204
AHOH793
AHOH996
BMET1
BGLU2
BASP4
BARG6

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

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PDB entries from 2024-10-09

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