Structure of PDB 5mac Chain E

Receptor sequence
>5macE (length=472) Species: 29291 (Methanococcoides burtonii) [Search protein sequence]
SLIYEDLVKSLDSKQQAYVDLKLPDPTNGEFLLAVFHMIPGGDLNVLQAA
AEIAAESSTGTNIKVSTETAFSRTMNARVYQLDLERELVWIAYPWRLFDR
GGNVQNILTYIIGNILGMKEIQALKLMDIWFPPSMLEQYDGPSYTVDDMR
KYLDVYDRPILGTIVKPKMGLTSAEYAEVCYDFWVGGGDFVKNDEPQANQ
DFCPYEKMVAHVKEAMDKAVKETGQKKVHSFNVSAADFDTMIERCEMITN
AGFEPGSYAFLIDGITAGWMAVQTLRRRYPDVFLHFHRAAHGAFTRQENP
IGFSVLVLSKFARLAGASGIHTGTAGIGKMKGTPAEDVVAAHSIQYLKSP
GHFFEQTWSKIMDTDKDVINLVNEDLAHHVILEDDSWRAMKKCCPIVSGG
LNPVKLKPFIDVMENVDFITTMGSGVHSHPGGTQSGAKALVQACDAYLQG
MDIEEYAKDHKELAEAIEFYLN
3D structure
PDB5mac A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic.
ChainE
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K167 K193 N194 D195 E196 H288 H322 K330
Catalytic site (residue number reindexed from 1) K166 K192 N193 D194 E195 H287 H321 K329
Enzyme Commision number 4.1.1.39: ribulose-bisphosphate carboxylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CAP E I165 K167 K169 K193 E196 H288 R289 H322 K330 M331 S399 G400 G401 G424 S425 I164 K166 K168 K192 E195 H287 R288 H321 K329 M330 S398 G399 G400 G423 S424
BS02 MG E K193 D195 E196 K192 D194 E195
BS03 MG E D366 D368 D365 D367
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016829 lyase activity
GO:0016984 ribulose-bisphosphate carboxylase activity
GO:0046872 metal ion binding
Biological Process
GO:0015977 carbon fixation

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Molecular Function
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Biological Process
External links
PDB RCSB:5mac, PDBe:5mac, PDBj:5mac
PDBsum5mac
PubMed28154188
UniProtQ12TQ0

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