Structure of PDB 5ks8 Chain C

Receptor sequence
>5ks8C (length=603) Species: 265072 (Methylobacillus flagellatus KT) [Search protein sequence]
KVHVTDVVLRDGHQSLIATRMRTDDMLPICSKLDAVGYWSLEAWGGATFD
ACVRYLREDPWERLKKLRKALPNSRLQMLLRGQNLLGYRHYSDDVVRAFV
QKSADNGIDVFRIFDAMNDLRNLKVSIESVKAVGKHAEGTISYTTSPVHD
IPYFVNLAKELESFGCDTIAIKDMASLLTPQVTGDLVKALREAVSLPIHL
HAHATSGLASMSIQRAVDNGVAIVDGCISSFAEGASLPATESIVAALKGT
EYDTGLDIGLLQEISAYFREVRKKYWQFESEFTGVDTRVLVNQVPGGMIS
NLSNQLKEQGALDRMDAVLDEIPRVREDLGYPPLVTPTSQIVGTQAVLNV
MTGARYKSVTNEVKNYLLGHYGKAPSTVNPDVRNLAVGNAQVIECRPADL
LTAEMEKLRNEVEGLAASAADVLTYAMFPDLAKTFLQERNAGSLKPEPLL
DKEAVTSRESHSRFAPTEFNVTLHGETFHIKLTGSGHHGEEQRPFYVSVD
GVTEEVVVEILNEAKRKASSAASSGRPRPTHAGCVTTAMPGTIVDVKVNV
GDKVSAGDAVLVIEAMKMENEIQASKSGVVVAINVKKGDSVTPDEALLEI
QPD
3D structure
PDB5ks8 A distinct holoenzyme organization for two-subunit pyruvate carboxylase.
ChainC
Resolution3.01 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D13 D117 K174 H203 H205
Catalytic site (residue number reindexed from 1) D11 D115 K172 H201 H203
Enzyme Commision number ?
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 PYR C L81 R83 F116 M176 L79 R81 F114 M174
BS02 MN C D13 K174 H203 H205 D11 K172 H201 H203
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5ks8, PDBe:5ks8, PDBj:5ks8
PDBsum5ks8
PubMed27708276
UniProtQ1H157

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