Structure of PDB 5c2g Chain D

Receptor sequence
>5c2gD (length=461) Species: 96 (Gallionella) [Search protein sequence]
GSHMDQSNRYADLSLKEEDLIKGGNHILVAYTMEPAAGVGYLEAAAHIAA
ESSTGTNVEVSTTDEFTKGVDALVYFIDEAKGIMKVAYPNDLFDRNVTDG
RVMIVSFLTLCIGNNQGMGDIANLQMQDFYVPPRMLQLFDGPAKDISDLW
RILGRPVKDGGYISGTIIKPKLGLRPEPFAKAAYQFWLGGDFIKNDEPQG
NQVFCPIKKVLPLVYDSLKRAQDETGQAKLFSMNITADDHYEMCARADFA
LETFGPDADKVAFLVDGFVGGPGMVTTARRQYPSQYLHYHRAGHGMVTSP
SSKRGYTAFVLAKMSRLQGASGIHVGTMGYGKMEGGKDDRIIAYMIERDS
CTGPFYHQEWYGMKPTTPIISGGMNALRLPGFFENLGHGNVINTAGGGSY
GHIDSPAAGAVSLRQAYECWKAGADPIEWAKEHKEFARAFESFPKDADKL
FPGWREKLGVH
3D structure
PDB5c2g Functional metagenomic selection of ribulose 1, 5-bisphosphate carboxylase/oxygenase from uncultivated bacteria.
ChainD
Resolution2.597 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 D I164 K166 K168 K191 E194 R288 H321 K329 S368 G369 G370 A392 G393 G394 I167 K169 K171 K194 E197 R291 H324 K332 S371 G372 G373 A395 G396 G397
BS02 MG D K191 D193 E194 K194 D196 E197
BS03 CAP D T53 N111 T56 N114
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5c2g, PDBe:5c2g, PDBj:5c2g
PDBsum5c2g
PubMed26617072
UniProtA0A0X1KHE5

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