Structure of PDB 4xc6 Chain A

Receptor sequence

>4xc6A (length=1067) Species: 266264 (Cupriavidus metallidurans CH34)

RGPANKVRFVTAASLFDGHDASINIMRRILQSQGCEVIHLGHNRSVQEVV
TAALQEDVQGIAISSYQGGHVEYFKYMIDLLREHGGEHIQVFGGGGGVIV
PDEIRELQAYGVARIYSPEDGQRMGLAGMITDMAQRCDIDLTRYAPTTLD
TVVAGDRRALAQLITALENGKADPELVSALHAQAKAAAVPVLGITGTGGA
GKSSLTDELIRRFRLDQDDALSIAVISIDPSRRKSGGALLGDRIRMNAIN
HPNIFMRSLATREAGSEISQALPDVIAACKAARFDLVIVETSGIGQGDAA
IVPHVDLSLYVMTPEFGAASQLEKIDMLDFADFVAINKFDRKGAQDAWRD
VAKQVQRNREQWHSRAEDMPVYGTQASRFNDDGVTMLYQGLVGALGARGM
SLKPGTLPNLEGRISTGQNVIVPPARSRYLAELADTVRAYHRRVVAQSKL
ARERQQLRAAHDMLQGAGHESAALETLASERDVSLGAVERKLLAMWPQMQ
QAYSGDEYVVIRTGLISTTLSGTKIRKVVLPRFEDEGEILKWLMRENVPG
SFPYTAGVFAFKREGEDPTRMFAGEGDAFRTNRRFKLVSEGMEAKRLSTA
FDSVTLYGEDPHERPDIYGKVGNSGVSIATLEDMKVLYDGFDLTNPSTSV
SMTINGPAPTILAMFMNTAIDQQIDRFRADNGRDPTADEEAKIRAWVLQN
VRGTVQADILKEDQGQNTCIFSTEFSLKVMGDIQEYFVHHQVRNFYSVSI
SGYHIAEAGANPISQLAFTLANGFTYVEAYLARGMHIDDFAPNLSFFFSN
GMDPEYSVLGRVARRIWAVTMRDKYGANDRSQKLKYHIQTSGRSLHAQEI
DFNDIRTTLQALIAIYDNCNSLHTNAYDEAITTPTAESVRRALAIQLIIN
REWGVAKCENPNQGSFLIEELTDLVEEAVLQEFERIAERGGVLGAMETGY
QRGKIQEESLYYEQLKHDGTLPIIGVNTFRNPNGDPTPQTLELARSSEDE
KQSQLHRLTEFHGAHQADAEAMLARLRQAVIDNRNVFAVLMDAVRVCSLG
QITHALFEVGGQYRRNM

3D structure

• PDB: 4xc6 Visualization of a radical B12 enzyme with its G-protein chaperone.
• Chain: A
• Resolution: 3.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K26 F598 Y779 H780
• Catalytic site (residue number reindexed from 1): K6 F572 Y753 H754
• Enzyme Commision number: 3.6.5.-
  5.4.99.13: isobutyryl-CoA mutase.

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	B12	A	G38 H39 D40 A41 S42 M46 Y86 Q87 G114 G116 V118 Y136 S137 P138 M149 F627 L632 S650 Q742 H780 E783 A784 G868 R869 E905 A906 T908 H993	G18 H19 D20 A21 S22 M26 Y66 Q67 G94 G96 V98 Y116 S117 P118 M129 F601 L606 S624 Q716 H754 E757 A758 G842 R843 E879 A880 T882 H967
BS02	GDP	A	G219 G221 K222 S223 S224 R265 N357 K358 D360 Q395 S397 E973	G199 G201 K202 S203 S204 R245 N337 K338 D340 Q375 S377 E947
BS03	MG	A	S223 D262 E310	S203 D242 E290
BS04	MG	A	D249 D262 E310	D229 D242 E290

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0003924 GTPase activity
• GO:0004494 methylmalonyl-CoA mutase activity
• GO:0005525 GTP binding
• GO:0016787 hydrolase activity
• GO:0016853 isomerase activity
• GO:0016866 intramolecular transferase activity
• GO:0031419 cobalamin binding
• GO:0034784 pivalyl-CoA mutase activity
• GO:0046872 metal ion binding
• GO:0047727 isobutyryl-CoA mutase activity

Biological Process

• GO:0006637 acyl-CoA metabolic process

External links

• PDB: RCSB:4xc6, PDBe:4xc6, PDBj:4xc6
• PDBsum: 4xc6
• PubMed: 25675500
• UniProt: Q1LRY0|ICMF_CUPMC Fused isobutyryl-CoA mutase (Gene Name=icmF)