Structure of PDB 5c2g Chain B

Receptor sequence
>5c2gB (length=454) Species: 96 (Gallionella) [Search protein sequence]
QSNRYADLSLKEEDLIKGGNHILVAYTMEPAAGVGYLEAAAHIAAESSTG
TNVEVSTTDEFTKGVDALVYFIDEAKGIMKVAYPNDLFDRNVTDGRVMIV
SFLTLCIGNNQGMGDIANLQMQDFYVPPRMLQLFDGPAKDISDLWRILGR
PVKDGGYISGTIIKPKLGLRPEPFAKAAYQFWLGGDFIKNDEPQGNQVFC
PIKKVLPLVYDSLKRAQDETGQAKLFSMNITADDHYEMCARADFALETFG
PDADKVAFLVDGFVGGPGMVTTARRQYPSQYLHYHRAGHGMVTSPSSKRG
YTAFVLAKMSRLQGASGIHVGTMGYGKMEGGKDDRIIAYMIERDSCTGPF
YHQEWYGMKPTTPIISGGMNALRLPGFFENLGHGNVINTAGGGSYGHIDS
PAAGAVSLRQAYECWKAGADPIEWAKEHKEFARAFESFPKDADKLFPGWR
EKLG
3D structure
PDB5c2g Functional metagenomic selection of ribulose 1, 5-bisphosphate carboxylase/oxygenase from uncultivated bacteria.
ChainB
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) K164 K189 N190 D191 E192 H285 H319 K327
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 B I164 K166 K168 K191 E194 R288 H321 K329 M330 S368 G369 G370 G393 G394 I162 K164 K166 K189 E192 R286 H319 K327 M328 S366 G367 G368 G391 G392
BS02 MG B K191 D193 E194 K189 D191 E192
BS03 CAP B T53 N111 T51 N109
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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