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3DO6

Crystal structure of Putative Formyltetrahydrofolate Synthetase (TM1766) from THERMOTOGA MARITIMA at 1.85 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004329molecular_functionformate-tetrahydrofolate ligase activity
A0005524molecular_functionATP binding
A0006730biological_processone-carbon metabolic process
A0016874molecular_functionligase activity
A0035999biological_processtetrahydrofolate interconversion
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 Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 543
ChainResidue
AHOH1030
BILE136
BASN140
BHOH586
BHOH844

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 544
ChainResidue
BSER172
BPHE176
AASP145
ATHR147
AARG148
BLYS137

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 545
ChainResidue
AARG148
BLYS137
BSER172
BALA173
BHOH782

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 543
ChainResidue
APHE500
AHOH1027

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 544
ChainResidue
ALEU499

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 546
ChainResidue
BARG82
BPHE260
BALA261
BGLY288
BPHE289

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 545
ChainResidue
AILE136
AASN140
APHE176
AHOH663
AHOH888
AHOH1030

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 546
ChainResidue
ALYS137
ASER172
APHE176
BASP145
BTHR147
BARG148

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 547
ChainResidue
AHIS135
ALEU226
AHOH845
BHOH871

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 547
ChainResidue
BHIS135
BASP225
BLEU226

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 549
ChainResidue
BPHE150
BPHE500
BHOH839

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 548
ChainResidue
ALEU11
AGLU12

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 550
ChainResidue
AGLY170
BSER164
BGLU179

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 551
ChainResidue
AARG349
ALEU387
BLEU423
BHOH886
BHOH925

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 552
ChainResidue
AGLU109
BTYR21
BHOH835
BHOH883

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 549
ChainResidue
ATYR21
AASP238
AHOH899
BTYR21
BGLY22
BGLU109

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 553
ChainResidue
BASN529
BHOH759

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 554
ChainResidue
BASP41
BGLY42
BASP417

Functional Information from PROSITE/UniProt
site_idPS00721
Number of Residues11
DetailsFTHFS_1 Formate--tetrahydrofolate ligase signature 1. GLKGGATGGGR
ChainResidueDetails
AGLY91-ARG101

site_idPS00722
Number of Residues12
DetailsFTHFS_2 Formate--tetrahydrofolate ligase signature 2. VATVRALKyHGG
ChainResidueDetails
AVAL316-GLY327

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01543
ChainResidueDetails
ATHR53
BTHR53

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eg7
ChainResidueDetails
ALYS59

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eg7
ChainResidueDetails
BLYS59

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PDB entries from 2024-07-17

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