Structure of PDB 8sac Chain D

Receptor sequence
>8sacD (length=391) Species: 1028307 (Klebsiella aerogenes KCTC 2190) [Search protein sequence]
HLDTALVNAGRRKKYTQGSVNSVIQRASSLVFDTVEAKKHATRNRAKGEL
FYGRRGTLTHFSLQEAMCELEGGAGCALFPCGAAAVANTILAFVEQGDHV
LMTNTAYEPSQDFCTKILAKLGVTTGWFDPLIGADIANLIQPNTKVVFLE
SPGSITMEVHDVPAIVAAVRRVAPEAIIMIDNTWAAGVLFKALDFGIDIS
IQAATKYLIGHSDGMIGTAVANARCWEQLCENAYLMGQMIDADTAYMTSR
GLRTLGVRLRQHHESSLRVAEWLAQHPQVARVNHPALPGSKGHEFWKRDF
SGSSGLFSFVLNKRLTDAELAAYLDNFSLFSMAYSWGGFESLILANQPEH
IAAIRPEAEVDFSGTLIRLHIGLENVDDLLADLAAGFARIV
3D structure
PDB8sac Crystal Structure of Cystathionine beta lyase from Klebsiella aerogenes (P21212 form)
ChainD
Resolution1.8 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 D Y56 R58 Y52 R54
BS02 PLP D C85 G86 A87 Y111 D185 A207 T209 K210 M219 W340 C81 G82 A83 Y107 D181 A203 T205 K206 M215 W336
BS03 MG D A356 R359 A362 A352 R355 A358
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:8sac, PDBe:8sac, PDBj:8sac
PDBsum8sac
PubMed
UniProtA0A0H3FMF8

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