Structure of PDB 8sae Chain B

Receptor sequence
>8saeB (length=393) Species: 1028307 (Klebsiella aerogenes KCTC 2190) [Search protein sequence]
DKHLDTALVNAGRRKKYTQGSVNSVIQRASSLVFDTVEAKKHATRNRAKG
ELFYGRRGTLTHFSLQEAMCELEGGAGCALFPCGAAAVANTILAFVEQGD
HVLMTNTAYEPSQDFCTKILAKLGVTTGWFDPLIGADIANLIQPNTKVVF
LESPGSITMEVHDVPAIVAAVRRVAPEAIIMIDNTWAAGVLFKALDFGID
ISIQAATKYLIGHSDGMIGTAVANARCWEQLCENAYLMGQMIDADTAYMT
SRGLRTLGVRLRQHHESSLRVAEWLAQHPQVARVNHPALPGSKGHEFWKR
DFSGSSGLFSFVLNKRLTDAELAAYLDNFSLFSMAYSWGGFESLILANQP
EHIAAIRPEAEVDFSGTLIRLHIGLENVDDLLADLAAGFARIV
3D structure
PDB8sae Crystal Structure of Cystathionine beta lyase from Klebsiella aerogenes, PLP and Hepes bound (C2 form)
ChainB
Resolution1.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.4.1.8: Transferred entry: 4.4.1.13.
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 PLP B C85 G86 A87 Y111 D185 A207 T209 K210 M219 W340 C83 G84 A85 Y109 D183 A205 T207 K208 M217 W338
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0046872 metal ion binding
GO:0047804 cysteine-S-conjugate beta-lyase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0019346 transsulfuration
GO:0019450 L-cysteine catabolic process to pyruvate

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Molecular Function
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Biological Process
External links
PDB RCSB:8sae, PDBe:8sae, PDBj:8sae
PDBsum8sae
PubMed
UniProtA0A0H3FMF8

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