Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1RU1

CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK(V83G/DEL84-89) WITH MGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.40 ANGSTROM RESOLUTION (MONOCLINIC FORM)

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
A0016740molecular_functiontransferase activity
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003848molecular_function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
B0005524molecular_functionATP binding
B0009396biological_processfolic acid-containing compound biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 161
ChainResidue
AASP95
AASP97
AMG162
AAPC171
AHOH413
AHOH423

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 162
ChainResidue
AAPC171
APH2181
AHOH403
AASP95
AASP97
AMG161

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 163
ChainResidue
ALYS119
APHE137
APRO138
AASP139

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 361
ChainResidue
BASP295
BASP297
BMG362
BAPC371
BHOH426
BHOH668

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 362
ChainResidue
BASP295
BASP297
BMG361
BAPC371
BPH2381
BHOH401

site_idAC6
Number of Residues26
DetailsBINDING SITE FOR RESIDUE APC A 171
ChainResidue
AGLN74
AASP95
AASP97
AILE98
AARG110
ALEU111
ATHR112
AVAL113
AHIS115
ATYR116
AARG121
AMG161
AMG162
APH2181
AHOH403
AHOH413
AHOH423
AHOH442
AHOH473
AHOH539
AHOH540
AHOH651
AHOH681
AHOH682
AHOH798
AHOH818

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PH2 A 181
ChainResidue
ATHR42
APRO43
ATYR53
AASN55
AASP95
APHE123
AMG162
AAPC171
AHOH403
AHOH640
AHOH708
AHOH713
AHOH818

site_idAC8
Number of Residues27
DetailsBINDING SITE FOR RESIDUE APC B 371
ChainResidue
BLEU270
BASP295
BASP297
BILE298
BARG310
BLEU311
BTHR312
BHIS315
BTYR316
BARG321
BHIS348
BMG361
BMG362
BPH2381
BHOH401
BHOH415
BHOH420
BHOH425
BHOH426
BHOH427
BHOH514
BHOH515
BHOH524
BHOH530
BHOH668
BHOH688
BHOH772

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PH2 B 381
ChainResidue
BASP295
BPHE323
BMG362
BAPC371
BHOH401
BHOH446
BHOH461
BHOH588
BTHR242
BPRO243
BLEU245
BTYR253
BASN255

Functional Information from PROSITE/UniProt
site_idPS00794
Number of Residues12
DetailsHPPK 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase signature. RgGPRtlDLDIM
ChainResidueDetails
AARG82-MET99

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hka
ChainResidueDetails
AARG92
AARG82

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hka
ChainResidueDetails
BARG292
BARG282

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

site_idMCSA2
Number of Residues4
DetailsM-CSA 151
ChainResidueDetails
BARG282electrostatic stabiliser, hydrogen bond donor
BARG292electrostatic stabiliser, hydrogen bond donor
BASP295metal ligand
BASP297metal ligand

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon