Structure of PDB 5c2g Chain E

Receptor sequence

>5c2gE (length=457) Species: 96 (Gallionella)

GSHMDQSNRYADLSLKEEDLIKGGNHILVAYTMEPAAGVGYLEAAAHIAA
ESSTGTNVEVSTTDEFTKGVDALVYFIDEAKGIMKVAYPNDLFDRNVTDG
RVMIVSFLTLCIGNNQGMGDIANLQMQDFYVPPRMLQLFDGPAKDISDLW
RILGRPVKDGGYISGTIIKPKLGLRPEPFAKAAYQFWLGGDFIKNDEPQG
NQVFCPIKKVLPLVYDSLKRAQDETGQAKLFSMNITADDHYEMCARADFA
LETFGPDADKVAFLVDGFVGGPGMVTTARRQYPSQYLHYHRAGHGMVTSP
SSKRGYTAFVLAKMSRLQGASGIHVGTMGYGKMEGGKDDRIIAYMIERDS
CTGPFYHQEWYGMKPTTPIISGGMNALRLPGFFENLGHGNVINTAGGGSY
GHIDSPAAGAVSLRQAYECWKAGADPIEWAKEHKEFARAFESFPKDADKL
FPGWREK

3D structure

• PDB: 5c2g Functional metagenomic selection of ribulose 1, 5-bisphosphate carboxylase/oxygenase from uncultivated bacteria.
• Chain: E
• Resolution: 2.597 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K166 K191 N192 D193 E194 H287 H321 K329
• Catalytic site (residue number reindexed from 1): K169 K194 N195 D196 E197 H290 H324 K332
• 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	T53 N111	T56 N114
BS02	CAP	E	I164 K166 K168 K191 E194 H287 R288 H321 K329 S368 G369 G370 G393 G394	I167 K169 K171 K194 E197 H290 R291 H324 K332 S371 G372 G373 G396 G397
BS03	MG	E	K191 D193 E194	K194 D196 E197

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0016984 ribulose-bisphosphate carboxylase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0015977 carbon fixation

External links

• PDB: RCSB:5c2g, PDBe:5c2g, PDBj:5c2g
• PDBsum: 5c2g
• PubMed: 26617072
• UniProt: A0A0X1KHE5