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3UD5

Crystal structure of E. coli HPPK in complex with bisubstrate analogue inhibitor J1A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003848molecular_function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
A0005524molecular_functionATP binding
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016301molecular_functionkinase activity
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE J1A A 171
ChainResidue
ATHR42
AARG110
ALEU111
ATHR112
APHE123
AHIS148
AEDO192
AHOH221
AHOH242
AHOH279
APRO43
ALEU45
ATYR53
AASN55
AGLN74
AASP95
AASP97
AILE98

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 191
ChainResidue
ATYR53
AARG92
AASP95

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 192
ChainResidue
AALA6
AGLY8
AASN55
AASP95
AASP97
APHE123
AMET124
AJ1A171

Functional Information from PROSITE/UniProt
site_idPS00794
Number of Residues12
DetailsHPPK 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase signature. RwGPRtlDLDIM
ChainResidueDetails
AARG88-MET99

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 151
ChainResidueDetails
AARG82electrostatic stabiliser, hydrogen bond donor
AARG92electrostatic stabiliser, hydrogen bond donor
AASP95metal ligand
AASP97metal ligand

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PDB entries from 2024-05-01

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