Structure of PDB 5cjt Chain B

Receptor sequence

>5cjtB (length=1060) Species: 266264 (Cupriavidus metallidurans CH34)

GPANKVRFVTAASLFDGHDASINIMRRILQSQGCEVIHLGHNRSVQEVVT
AALQEDVQGIAISSYQGGHVEYFKYMIDLLREHGGEHIQVFGGGGGVIVP
DEIRELQAYGVARIYSPEDGQRMGLAGMITDMAQRCDIDLTRYAPTTLDT
VVAGDRRALAQLITALENGKADPELVSALHAQAKAAAVPVLGITGTGGAG
KSSLTDELIRRFRLDQDDALSIAVISIDPSRRKSGGALLGDRIRMNAINH
PNIFMRSLATREAGSEISQALPDVIAACKAARFDLVIVETSGIGQGDAAI
VPHVDLSLYVMTPEFGAASQLEKIDMLDFADFVAINKFDRKGAQDAWRDV
AKQVQRNREQWHSRAEDMPVYGTQASRFNDDGVTMLYQGLVGALGARGMS
LKPGTLPNLEGRISTGQNVIVPPARSRYLAELADTVRAYHRRVVAQSKLA
RERQQLRAAHDMLQGAGHESAALETLASERDVSLGAVERKLLAMWPQMQQ
AYSGDEYVVKIRDKEIRTGLISTTLSGTKIRKVVLPRFEDEGEILKWLMR
ENVPGSFPYTAGVFAFKREGDPTRMFAGEGDAFRTNRRFKLVSEGMEAKR
LSTAFDSVTLYGEDPHERPDIYGKVGNSGVSIATLEDMKVLYDGFDLTNP
STSVSMTINGPAPTILAMFMNTAIDQQIDRFRADNGRDPTADEEAKIRAW
VLQNVRGTVQADILKEDQGQNTCIFSTEFSLKVMGDIQEYFVHHQVRNFY
SVSISGYHIAEAGANPISQLAFTLANGFTYVEAYLARGMHIDDFAPNLSF
FFSNGMDPEYSVLGRVARRIWAVTMRDKYGANDRSQKLKYHIQTSGRSLH
AQEIDFNDIRTTLQALIAIYDNCNSLHTNAYITTPTAESVRRALAIQLII
NREWGVAKCENPNQGSFLIEELTDLVEEAVLQEFERIAERGGVLGAMETG
YQRGKIQEESLYYEQLKHDGTLPIIGVNTFRNPNGLARSSEDEKQSQLHR
LTEFHGAHQADAEAMLARLRQAVIDNRNVFAVLMDAVRVCSLGQITHALF
EVGGQYRRNM

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): K26 F598 Y779 H780
• Catalytic site (residue number reindexed from 1): K5 F576 Y757 H758
• 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	B	H39 D40 A41 S42 M46 Y86 Q87 G114 G116 Y136 S137 G141 M149 Q742	H18 D19 A20 S21 M25 Y65 Q66 G93 G95 Y115 S116 G120 M128 Q720
BS02	CO6	B	F585 R856	F564 R834
BS03	GDP	B	G219 G221 K222 S223 S224 R265 N357 K358 D360 Q395 S397 E973 N1092	G198 G200 K201 S202 S203 R244 N336 K337 D339 Q374 S376 E948 N1059
BS04	MG	B	S223 D262 E310	S202 D241 E289
BS05	MG	B	I248 D249 D262 E310	I227 D228 D241 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)