Structure of PDB 5ks8 Chain D

Receptor sequence

>5ks8D (length=580) Species: 265072 (Methylobacillus flagellatus KT)

AKVHVTDVVLRDGHQSLIATRMRTDDMLPICSKLDAVGYWSLEAWGGATF
DACVRYLREDPWERLKKLRKALPNSRLQMLLRGQNLLGYRHYSDDVVRAF
VQKSADNGIDVFRIFDAMNDLRNLKVSIESVKAVGKHAEGTISYTTSPVH
DIPYFVNLAKELESFGCDTIAIKDMASLLTPQVTGDLVKALREAVSLPIH
LHAHATSGLASMSIQRAVDNGVAIVDGCISSFAEGASLPATESIVAALKG
TEYDTGLDIGLLQEISAYFREVRKKYWQFESEFTGVDTRVLVNQVPGGMI
SNLSNQLKEQGALDRMDAVLDEIPRVREDLGYPPLVTPTSQIVGTQAVLN
VMTGARYKSVTNEVKNYLLGHYGKAPSTVNPDVRNLAVGNAQVIECRPAD
LLTAEMEKLRNEVEGLAASAADVLTYAMFPDLAKTFLQERNAGSLKPEPL
LDKEAVTSRESHSRFAPTEFNVTLHGETFHIKLTPFYVSVDGVTEEVVVE
ILNRPRPTHAGCVTTAMPGTIVDVKVNVGDKVSAGDAVLVIEAMKMENEI
QASKSGVVVAINVKKGDSVTPDEALLEIQP

3D structure

• PDB: 5ks8 A distinct holoenzyme organization for two-subunit pyruvate carboxylase.
• Chain: D
• Resolution: 3.01 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D13 D117 K174 H203 H205
• Catalytic site (residue number reindexed from 1): D12 D116 K173 H202 H204

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	BTI	D	D52 Y57 M300 T338 S341 Q342	D51 Y56 M299 T337 S340 Q341
BS02	PYR	D	Q16 G48 L81 R83 T338	Q15 G47 L80 R82 T337
BS03	MN	D	D13 K174 H203 H205	D12 K173 H202 H204

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004736 pyruvate carboxylase activity
• GO:0008948 oxaloacetate decarboxylase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006814 sodium ion transport

External links

• PDB: RCSB:5ks8, PDBe:5ks8, PDBj:5ks8
• PDBsum: 5ks8
• PubMed: 27708276
• UniProt: Q1H157