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3QUS

Crystal Structure of N10-Formyltetrahydrofolate Synthetase with ATPgS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004329molecular_functionformate-tetrahydrofolate ligase activity
A0005524molecular_functionATP binding
A0006730biological_processone-carbon metabolic process
A0016874molecular_functionligase activity
A0035999biological_processtetrahydrofolate interconversion
B0000166molecular_functionnucleotide binding
B0004329molecular_functionformate-tetrahydrofolate ligase activity
B0005524molecular_functionATP binding
B0006730biological_processone-carbon metabolic process
B0016874molecular_functionligase activity
B0035999biological_processtetrahydrofolate interconversion
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
ALYS74
AARG97
AGLY303
APHE304
AAGS700
AHOH814

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AHOH736
ASER44
AASP46
ALYS256

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
AARG175
AARG178
AGLY537

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 605
ChainResidue
ASER446
AARG505
AARG507
AHOH626

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AGS A 700
ChainResidue
AGLU72
AGLY73
ALYS74
ATHR75
ATHR76
AGLY113
AASN382
AALA383
APHE384
APRO385
ATRP412
ASO4601
AHOH791

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TOE A 701
ChainResidue
AARG162
AILE164
AGLU194
AHOH789

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE TOE A 702
ChainResidue
ATYR482

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 602
ChainResidue
BARG175
BARG178
BMET533
BGLY537

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
BLYS74
BARG97
BGLY303
BPHE304

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AGS B 700
ChainResidue
BGLU9
BGLY71
BGLU72
BGLY73
BLYS74
BTHR75
BTHR76
BGLY113
BALA383
BPHE384
BTRP412

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MAE B 702
ChainResidue
BSER44
BLYS252
BLYS256

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MAE B 703
ChainResidue
BARG162
BILE164
BGLU194
BHOH606
BHOH622

Functional Information from PROSITE/UniProt
site_idPS00721
Number of Residues11
DetailsFTHFS_1 Formate--tetrahydrofolate ligase signature 1. GIKGGAAGGGY
ChainResidueDetails
AGLY106-TYR116

site_idPS00722
Number of Residues12
DetailsFTHFS_2 Formate--tetrahydrofolate ligase signature 2. VATVRALKmHGG
ChainResidueDetails
AVAL331-GLY342

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01543","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 385
ChainResidueDetails
ALYS74electrostatic stabiliser
ATHR76steric role
AARG97electrostatic stabiliser
ALYS108electrostatic stabiliser
AALA276electrostatic stabiliser
APHE304electrostatic stabiliser
APHE384activator
ATRP412activator

site_idMCSA2
Number of Residues8
DetailsM-CSA 385
ChainResidueDetails
BLYS74electrostatic stabiliser
BTHR76steric role
BARG97electrostatic stabiliser
BLYS108electrostatic stabiliser
BALA276electrostatic stabiliser
BPHE304electrostatic stabiliser
BPHE384activator
BTRP412activator

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PDB entries from 2025-12-24

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