Structure of PDB 3b1d Chain C

Receptor sequence
>3b1dC (length=386) Species: 1328 (Streptococcus anginosus) [Search protein sequence]
KYNFQTAPNRLSHHTYKWKETETDPQLLPAWIADMDFEVMPEVKQAIHDY
AEQLVYGYTYASDELLQAVLDWEKSEHQYSFDKEDIVFVEGVVPAISIAI
QAFTKEGEAVLINSPVYPPFARSVRLNNRKLVSNSLKEENGLFQIDFEQL
ENDIVENDVKLYLLCNPHNPGGRVWEREVLEQIGHLCQKHHVILVSDEIH
QDLTLFGHEHVSFNTVSPDFKDFALVLSSATKTFNIAGTKNSYAIIENPT
LCAQFKHQQLVNNHHEVSSLGYIATETAYRYGKPWLVALKAVLEENIQFA
VEYFAQEAPRLKVMKPQGTYLIWLDFSDYGLTDDALFTLLHDQAKVILNR
GSDYGSEGELHARLNIAAPKSLVEEICKRIVCCLPK
3D structure
PDB3b1d Structural insights into catalysis by beta C-S lyase from Streptococcus anginosus
ChainC
Resolution1.66 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y119 D199 I201
Catalytic site (residue number reindexed from 1) Y117 D197 I199
Enzyme Commision number 4.4.1.13: cysteine-S-conjugate beta-lyase.
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 C G93 V94 V95 Y119 D199 I201 H202 K234 G91 V92 V93 Y117 D197 I199 H200 K232
BS02 PLS C I34 A35 V94 Y119 N171 D199 I201 H202 K234 R365 I32 A33 V92 Y117 N169 D197 I199 H200 K232 R363
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3b1d, PDBe:3b1d, PDBj:3b1d
PDBsum3b1d
PubMed22674431
UniProtA6BMJ3

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