Structure of PDB 5cjt Chain A

Receptor sequence

>5cjtA (length=1062) Species: 266264 (Cupriavidus metallidurans CH34)

RGPANKVRFVTAASLFDGHDASINIMRRILQSQGCEVIHLGHNRSVQEVV
TAALQEDVQGIAISSYQGGHVEYFKYMIDLLREHGGEHIQVFGGGGGVIV
PDEIRELQAYGVARIYSPEDGQRMGLAGMITDMAQRCDIDLTRYAPTTLD
TVVAGDRRALAQLITALENGKADPELVSALHAQAKAAAVPVLGITGTGGA
GKSSLTDELIRRFRLDQDDALSIAVISIDPSRRKSGGALLGDRIRMNAIN
HPNIFMRSLATREASEISQALPDVIAACKAARFDLVIVETSGIGQGDAAI
VPHVDLSLYVMTPEFGAASQLEKIDMLDFADFVAINKFDRKGAQDAWRDV
AKQVQRNREQWHSRAEDMPVYGTQASRFNDDGVTMLYQGLVGALGARGMS
LKPGTLPNLEGRISTGQNVIVPPARSRYLAELADTVRAYHRRVVAQSKLA
RERQQLRAAHDMLQGAGHESAALETLASERDVSLGAVERKLLAMWPQMQQ
AYSGDEYVRTGLISTTLSGTKIRKVVLPRFEDEGEILKWLMRENVPGSFP
YTAGVFAFKREGEDPTRMFAGEGDAFRTNRRFKLVSEGMEAKRLSTAFDS
VTLYGEDPHERPDIYGKVGNSGVSIATLEDMKVLYDGFDLTNPSTSVSMT
INGPAPTILAMFMNTAIDQQIDRFRADNGRDPTADEEAKIRAWVLQNVRG
TVQADILKEDQGQNTCIFSTEFSLKVMGDIQEYFVHHQVRNFYSVSISGY
HIAEAGANPISQLAFTLANGFTYVEAYLARGMHIDDFAPNLSFFFSNGMD
PEYSVLGRVARRIWAVTMRDKYGANDRSQKLKYHIQTSGRSLHAQEIDFN
DIRTTLQALIAIYDNCNSLHTNAYDEAITTPTAESVRRALAIQLIINREW
GVAKCENPNQGSFLIEELTDLVEEAVLQEFERIAERGGVLGAMETGYQRG
KIQEESLYYEQLKHDGTLPIIGVNTFRNPNGDPQTLELARSSEDEKQSQL
HRLTEFHGAHQADAEAMLARLRQAVIDNRNVFAVLMDAVRVCSLGQITHA
LFEVGGQYRRNM

3D structure

• PDB: 5cjt Structural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases.
• Chain: A
• Resolution: 3.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K26 F598 Y779 H780
• Catalytic site (residue number reindexed from 1): K6 F569 Y750 H751
• 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 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 F598 L603 S621 Q713 H751 E754 A755 G839 R840 E876 A877 T879 H964
BS02	CO6	A	F585 F587 R589 R596 F598 R622 S677 T679 R728 T730 Q732 Y772 Y779 H780 S821 F823 R856 K861 H863	F556 F558 R560 R567 F569 R593 S648 T650 R699 T701 Q703 Y743 Y750 H751 S792 F794 R827 K832 H834
BS03	GDP	A	G219 G221 K222 S223 S224 R265 N357 K358 D360 Q395 S397 E973	G199 G201 K202 S203 S204 R245 N336 K337 D339 Q374 S376 E944
BS04	MG	A	S223 D262 E310	S203 D242 E289
BS05	MG	A	D249 D262 E310	D229 D242 E289

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:5cjt, PDBe:5cjt, PDBj:5cjt
• PDBsum: 5cjt
• PubMed: 26318610
• UniProt: Q1LRY0|ICMF_CUPMC Fused isobutyryl-CoA mutase (Gene Name=icmF)