Structure of PDB 5mac Chain D

Receptor sequence
>5macD (length=473) Species: 29291 (Methanococcoides burtonii) [Search protein sequence]
MSLIYEDLVKSLDSKQQAYVDLKLPDPTNGEFLLAVFHMIPGGDLNVLQA
AAEIAAESSTGTNIKVSTETAFSRTMNARVYQLDLERELVWIAYPWRLFD
RGGNVQNILTYIIGNILGMKEIQALKLMDIWFPPSMLEQYDGPSYTVDDM
RKYLDVYDRPILGTIVKPKMGLTSAEYAEVCYDFWVGGGDFVKNDEPQAN
QDFCPYEKMVAHVKEAMDKAVKETGQKKVHSFNVSAADFDTMIERCEMIT
NAGFEPGSYAFLIDGITAGWMAVQTLRRRYPDVFLHFHRAAHGAFTRQEN
PIGFSVLVLSKFARLAGASGIHTGTAGIGKMKGTPAEDVVAAHSIQYLKS
PGHFFEQTWSKIMDTDKDVINLVNEDLAHHVILEDDSWRAMKKCCPIVSG
GLNPVKLKPFIDVMENVDFITTMGSGVHSHPGGTQSGAKALVQACDAYLQ
GMDIEEYAKDHKELAEAIEFYLN
3D structure
PDB5mac A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic.
ChainD
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) K167 K193 N194 D195 E196 H288 H322 K330
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 MG D E179 D183 E179 D183
BS02 CAP D T62 N115 T62 N115
BS03 CAP D I165 K167 K169 K193 D195 H288 R289 H322 K330 M331 S399 G400 G424 I165 K167 K169 K193 D195 H288 R289 H322 K330 M331 S399 G400 G424
BS04 MG D K193 D195 E196 K193 D195 E196
BS05 MG D D366 D368 D366 D368
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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