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3UDE

Crystal structure of E. coli HPPK in complex with bisubstrate analogue inhibitor J1B

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE J1B A 171
ChainResidue
ALYS23
AGLY90
AASP95
AASP97
AILE98
AARG110
ALEU111
ATHR112
ATYR116
APHE123
AHIS148
ATHR42
AACT191
AHOH221
AHOH236
APRO43
ALEU45
ATYR53
AASN55
ALEU70
AGLN74
ATRP89

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 191
ChainResidue
AGLY8
AASN55
AASP95
AASP97
APHE123
AJ1B171
AHOH284

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

218853

PDB entries from 2024-04-24

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