Structure of PDB 5cjw Chain A

Receptor sequence

>5cjwA (length=1063) Species: 266264 (Cupriavidus metallidurans CH34)

RGPANKVRFVTAASLFDGHDASINIMRRILQSQGCEVIHLGHNRSVQEVV
TAALQEDVQGIAISSYQGGHVEYFKYMIDLLREHGGEHIQVFGGGGGVIV
PDEIRELQAYGVARIYSPEDGQRMGLAGMITDMAQRCDIDLTRYAPTTLD
TVVAGDRRALAQLITALENGKADPELVSALHAQAKAAAVPVLGITGTGGA
GKSSLTDELIRRFRLDQDDALSIAVISIDPSRRKSGGALLGDRIRMNAIN
HPNIFMRSLATREAGSEISQALPDVIAACKAARFDLVIVETSGIGQGDAA
IVPHVDLSLYVMTPEFGAASQLEKIDMLDFADFVAINKFDRKGAQDAWRD
VAKQVQRNREQWHSRAEDMPVYGTQASRFNDDGVTMLYQGLVGALGARGM
SLKPGTLPNLEGRISTGQNVIVPPARSRYLAELADTVRAYHRRVVAQSKL
ARERQQLRAAHDMLQGAGHESAALETLASERDVSLGAVERKLLAMWPQMQ
QAYSGDEYVIRTGLISTTLSGTKIRKVVLPRFEDEGEILKWLMRENVPGS
FPYTAGVFAFKREGEDPTRMFAGEGDAFRTNRRFKLVSEGMEAKRLSTAF
DSVTLYGEDPHERPDIYGKVGNSGVSIATLEDMKVLYDGFDLTNPSTSVS
MTINGPAPTILAMFMNTAIDQQIDRFRADNGRDPTADEEAKIRAWVLQNV
RGTVQADILKEDQGQNTCIFSTEFSLKVMGDIQEYFVHHQVRNFYSVSIS
GYHIAEAGANPISQLAFTLANGFTYVEAYLARGMHIDDFAPNLSFFFSNG
MDPEYSVLGRVARRIWAVTMRDKYGANDRSQKLKYHIQTSGRSLHAQEID
FNDIRTTLQALIAIYDNCNSLHTNAYDEAITTPTAESVRRALAIQLIINR
EWGVAKCENPNQGSFLIEELTDLVEEAVLQEFERIAERGGVLGAMETGYQ
RGKIQEESLYYEQLKHDGTLPIIGVNTFRNPNGDQTLELARSSEDEKQSQ
LHRLTEFHGAHQADAEAMLARLRQAVIDNRNVFAVLMDAVRVCSLGQITH
ALFEVGGQYRRNM

3D structure

• PDB: 5cjw 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 F571 Y752 H753
• 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 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 F600 L605 S623 Q715 H753 E756 A757 G841 R842 E878 A879 T881 H966
BS02	52O	A	F585 F587 R589 R596 F598 R622 S677 T679 R728 T730 Q732 Y772 Y779 H780 S821 F823 R856 K861 H863	F558 F560 R562 R569 F571 R595 S650 T652 R701 T703 Q705 Y745 Y752 H753 S794 F796 R829 K834 H836
BS03	GDP	A	G219 G221 K222 S223 S224 R265 N357 K358 D360 Q395 S397 N1092	G199 G201 K202 S203 S204 R245 N337 K338 D340 Q375 S377 N1062
BS04	MG	A	S223 D262 E310	S203 D242 E290
BS05	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:5cjw, PDBe:5cjw, PDBj:5cjw
• PDBsum: 5cjw
• PubMed: 26318610
• UniProt: Q1LRY0|ICMF_CUPMC Fused isobutyryl-CoA mutase (Gene Name=icmF)