Structure of PDB 3glm Chain A

Receptor sequence
>3glmA (length=562) Species: 1512 ([Clostridium] symbiosum) [Search protein sequence]
MYSMPGYFQNMPTIGKELVNPNPENEQEIKAVESDIHESIKKALDAGITS
EEKLNERGQLSAMQRINALIDPGTWCPLNSLFNPENNKFGTTNIVNGLGR
VDGKWVYIVASDNKKMAGAWVPGQAENLIRCSDAAKMMHLPLIYLLNCSG
VEFPNQDKVYPNRRGGGTPFFRNSELNQLGIPVIVGIYGTNPAGGGYHSI
SPTILIAHQDANMAVGGAGAEQIIAAQIENSKLKVPAPGSVPIHYDETGF
FREVYQNDLGVIDGIKKYISYLPAYNLEFFRVDTPKAPQLPAEDLYSIIP
MNQKRPYDIYEVIARLFDNSEFSEYKKGYGPEMVTGLAKVNGLLVGVIAN
VQGLLMNYPEYKQNSVGIGGKLYRQGLIKMNEFVTLCARDRIPLIWLQDT
TGIDVGDEAEKAELLGLGQSLIYSIENSKLPSLEITIRKASAAAHYVLGG
PQGNNTNVFSIGTGACEYYVMPGETAANAMYSRKLVKAQPIIGKMNDMIQ
MYTDKSRPKYCTEKGMVDEIVDMTEVRPYIQAFTEAAYQNPQSICPMHQM
LTPRSTREFETF
3D structure
PDB3glm An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V153 A195 G196 I420 A460 A461
Catalytic site (residue number reindexed from 1) V151 A193 G194 I403 A443 A444
Enzyme Commision number 4.1.1.70: Transferred entry: 7.2.4.5.
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 COO A R59 M118 A119 S151 G152 V153 E154 F155 Y162 T192 A195 G196 R57 M116 A117 S149 G150 V151 E152 F153 Y160 T190 A193 G194
BS02 COO A A460 V487 R500 A443 V470 R483
Gene Ontology
Molecular Function
GO:0004485 methylcrotonoyl-CoA carboxylase activity
GO:0016874 ligase activity
Biological Process
GO:0006552 L-leucine catabolic process
Cellular Component
GO:1905202 methylcrotonoyl-CoA carboxylase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3glm, PDBe:3glm, PDBj:3glm
PDBsum3glm
PubMed19654317
UniProtB7TVP1

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