Structure of PDB 5mac Chain A

Receptor sequence

>5macA (length=473) Species: 29291 (Methanococcoides burtonii)

MSLIYEDLVKSLDSKQQAYVDLKLPDPTNGEFLLAVFHMIPGGDLNVLQA
AAEIAAESSTGTNIKVSTETAFSRTMNARVYQLDLERELVWIAYPWRLFD
RGGNVQNILTYIIGNILGMKEIQALKLMDIWFPPSMLEQYDGPSYTVDDM
RKYLDVYDRPILGTIVKPKMGLTSAEYAEVCYDFWVGGGDFVKNDEPQAN
QDFCPYEKMVAHVKEAMDKAVKETGQKKVHSFNVSAADFDTMIERCEMIT
NAGFEPGSYAFLIDGITAGWMAVQTLRRRYPDVFLHFHRAAHGAFTRQEN
PIGFSVLVLSKFARLAGASGIHTGTAGIGKMKGTPAEDVVAAHSIQYLKS
PGHFFEQTWSKIMDTDKDVINLVNEDLAHHVILEDDSWRAMKKCCPIVSG
GLNPVKLKPFIDVMENVDFITTMGSGVHSHPGGTQSGAKALVQACDAYLQ
GMDIEEYAKDHKELAEAIEFYLN

3D structure

• PDB: 5mac A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic.
• Chain: A
• Resolution: 2.6 Å

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	CAP	A	I165 K167 K169 K193 D195 E196 H288 R289 H322 K330 S399 G400 G401 G424 S425	I165 K167 K169 K193 D195 E196 H288 R289 H322 K330 S399 G400 G401 G424 S425
BS02	MG	A	K193 D195 E196	K193 D195 E196
BS03	MG	A	D366 D368	D366 D368
BS04	MG	A	E179 D183	E179 D183

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

External links

• PDB: RCSB:5mac, PDBe:5mac, PDBj:5mac
• PDBsum: 5mac
• PubMed: 28154188
• UniProt: Q12TQ0