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3FA4

Crystal structure of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member, triclinic crystal form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0016787molecular_functionhydrolase activity
C0016829molecular_functionlyase activity
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0016787molecular_functionhydrolase activity
D0016829molecular_functionlyase activity
D0046872molecular_functionmetal ion binding
E0003824molecular_functioncatalytic activity
E0016787molecular_functionhydrolase activity
E0016829molecular_functionlyase activity
E0046872molecular_functionmetal ion binding
F0003824molecular_functioncatalytic activity
F0016787molecular_functionhydrolase activity
F0016829molecular_functionlyase activity
F0046872molecular_functionmetal ion binding
G0003824molecular_functioncatalytic activity
G0016787molecular_functionhydrolase activity
G0016829molecular_functionlyase activity
G0046872molecular_functionmetal ion binding
H0003824molecular_functioncatalytic activity
H0016787molecular_functionhydrolase activity
H0016829molecular_functionlyase activity
H0046872molecular_functionmetal ion binding
I0003824molecular_functioncatalytic activity
I0016787molecular_functionhydrolase activity
I0016829molecular_functionlyase activity
I0046872molecular_functionmetal ion binding
J0003824molecular_functioncatalytic activity
J0016787molecular_functionhydrolase activity
J0016829molecular_functionlyase activity
J0046872molecular_functionmetal ion binding
K0003824molecular_functioncatalytic activity
K0016787molecular_functionhydrolase activity
K0016829molecular_functionlyase activity
K0046872molecular_functionmetal ion binding
L0003824molecular_functioncatalytic activity
L0016787molecular_functionhydrolase activity
L0016829molecular_functionlyase activity
L0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP87
AASP89
AHOH765

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP87
BASP89
BHOH370
BHOH902
BHOH903

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 401
ChainResidue
CASP89
CASP87

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 401
ChainResidue
DASP87
DASP89
DHOH495
DHOH868
DHOH905

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG E 401
ChainResidue
EASP87
EASP89
EHOH760
EHOH869

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG F 401
ChainResidue
FASP59
FASP87
FASP89
FHOH840

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG G 401
ChainResidue
GASP87
GASP89
GHOH598
GHOH762
GHOH918
GHOH1071

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG H 401
ChainResidue
HASP59
HASP87
HASP89
HHOH873
HHOH884

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG I 401
ChainResidue
IASP87
IASP89

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG J 401
ChainResidue
JASP87
JASP89

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG K 401
ChainResidue
KASP59
KASP87
KASP89

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG L 401
ChainResidue
LASP59
LASP87
LASP89
LHOH304

Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KRCGHL
ChainResidueDetails
ALYS122-LEU127

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PDB entries from 2024-06-12

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