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1DY3

Ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue.

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
AASP95
AASP97
AATP200
A87Y201
AMG203
AHOH2141

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 203
ChainResidue
AMG202
AHOH2068
AHOH2136
AASP95
AASP97
AATP200

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP A 200
ChainResidue
AARG82
AARG84
AALA86
AGLU87
AARG88
ATRP89
AARG92
AASP95
AASP97
AILE98
AARG110
ALEU111
ATHR112
AHIS115
ATYR116
AARG121
A87Y201
AMG202
AMG203
AHOH2136
AHOH2138
AHOH2139
AHOH2140

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 87Y A 201
ChainResidue
ATHR42
APRO43
ALEU45
ATYR53
AASN55
ATRP89
AARG92
APHE123
AATP200
AMG202
AHOH2084
AHOH2103
AHOH2141

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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hka
ChainResidueDetails
AARG92
AARG82

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

222624

PDB entries from 2024-07-17

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