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3UDV

Crystal structure of E. coli HPPK in complex with bisubstrate analogue inhibitor J1C

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 Residues23
DetailsBINDING SITE FOR RESIDUE J1C A 171
ChainResidue
ALYS23
ATRP89
AGLY90
AARG92
AASP95
AASP97
AILE98
AARG110
ATHR112
APHE123
AACT191
ATHR42
AHOH232
AHOH254
AHOH255
AHOH263
APRO43
ALEU45
ATYR53
AASN55
AGLN74
AGLU77
AARG88

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 191
ChainResidue
AALA6
AGLY8
AASN55
AASP97
AMET124
AJ1C171
AHOH227

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

221051

PDB entries from 2024-06-12

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