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1SBQ

Crystal Structure of methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae at 2.2 resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016874molecular_functionligase activity
A0030272molecular_function5-formyltetrahydrofolate cyclo-ligase activity
A0035999biological_processtetrahydrofolate interconversion
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0009396biological_processfolic acid-containing compound biosynthetic process
B0016874molecular_functionligase activity
B0030272molecular_function5-formyltetrahydrofolate cyclo-ligase activity
B0035999biological_processtetrahydrofolate interconversion
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG115
AHOH527
AGLY117
APHE118
AGLY119
ALYS120
AGLY121
ATYR122
ATYR123
AHOH514

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BARG115
BPHE118
BGLY119
BLYS120
BGLY121
BTYR122
BTYR123
BASP124

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AGLU95
APRO96
AASN97
BASN97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16104022","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 541
ChainResidueDetails
AARG115electrostatic stabiliser, increase electrophilicity
AASP124metal ligand
AASP154metal ligand

site_idMCSA2
Number of Residues3
DetailsM-CSA 541
ChainResidueDetails
BARG115electrostatic stabiliser, increase electrophilicity
BASP124metal ligand
BASP154metal ligand

249697

PDB entries from 2026-02-25

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