Structure of PDB 3gma Chain B

Receptor sequence

>3gmaB (length=566) Species: 1512 ([Clostridium] symbiosum)

MYSMPGYFQNMPTIGKELVNPNPENEQEIKAVESDIHESIKKALDAGITS
EEKLNERGQLSAMQRINALIDPGTWCPLNSLFNPENNKFGTTNIVNGLGR
VDGKWVYIVASDNKKMAGAWVPGQAENLIRCSDAAKMMHLPLIYLLNCSG
VEFPNQDKVYPNRRGGGTPFFRNSELNQLGIPVIVGIYGTNPAGGGYHSI
SPTILIAHQDANMAVGGAGDDEAAEQIIAAQIENSKLKVPAPGSVPIHYD
ETGFFREVYQNDLGVIDGIKKYISYLPAYNLEFFRVDTPKAPQLPAEDLY
SIIPMNQKRPYDIYEVIARLFDNSEFSEYKKGYGPEMVTGLAKVNGLLVG
VIANVQGLLMNYPEYKQNSVGIGGKLYRQGLIKMNEFVTLCARDRIPLIW
LQDTTGIDVGDEAEKAELLGLGQSLIYSIENSKLPSLEITIRKASAAAHY
VLGGPQGNNTNVFSIGTGACEYYVMPGETAANAMYSRKLVKAQPIIGKMN
DMIQMYTDKSRPKYCTEKGMVDEIVDMTEVRPYIQAFTEAAYQNPQSICP
MHQMLTPRSTREFETF

3D structure

• PDB: 3gma An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases
• Chain: B
• Resolution: 2.6 Å

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 I407 A447 A448
• 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	GRA	B	M118 S151 G152 V153 E154 F155 T192 A195 G196	M116 S149 G150 V151 E152 F153 T190 A193 G194

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

External links

• PDB: RCSB:3gma, PDBe:3gma, PDBj:3gma
• PDBsum: 3gma
• PubMed: 19654317
• UniProt: B7TVP1