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1SBQ

Crystal Structure of methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae at 2.2 resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016874molecular_functionligase activity
A0030272molecular_function5-formyltetrahydrofolate cyclo-ligase activity
A0046872molecular_functionmetal ion binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0016874molecular_functionligase activity
B0030272molecular_function5-formyltetrahydrofolate cyclo-ligase activity
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 Residues6
DetailsBINDING:
ChainResidueDetails
ALYS3
AARG125
ATRP153
BLYS3
BARG125
BTRP153

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16104022
ChainResidueDetails
AGLU50
AGLU55
AASP124
AASP154
BGLU50
BGLU55
BASP124
BASP154

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AARG115
BARG115

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

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PDB entries from 2024-07-24

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