Structure of PDB 3b1e Chain B

Receptor sequence
>3b1eB (length=387) Species: 1328 (Streptococcus anginosus) [Search protein sequence]
SKYNFQTAPNRLSHHTYKWKETETDPQLLPAWIADMDFEVMPEVKQAIHD
YAEQLVYGYTYASDELLQAVLDWEKSEHQYSFDKEDIVFVEGVVPAISIA
IQAFTKEGEAVLINSPVYPPFARSVRLNNRKLVSNSLKEENGLFQIDFEQ
LENDIVENDVKLYLLCNPHNPGGRVWEREVLEQIGHLCQKHHVILVSDEI
HQDLTLFGHEHVSFNTVSPDFKDFALVLSSATKTFNIAGTKNSYAIIENP
TLCAQFKHQQLVNNHHEVSSLGYIATETAYRYGKPWLVALKAVLEENIQF
AVEYFAQEAPRLKVMKPQGTYLIWLDFSDYGLTDDALFTLLHDQAKVILN
RGSDYGSEGELHARLNIAAPKSLVEEICKRIVCCLPK
3D structure
PDB3b1e Structural insights into catalysis by beta C-S lyase from Streptococcus anginosus
ChainB
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y119 D199 I201
Catalytic site (residue number reindexed from 1) Y118 D198 I200
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 0JO B I34 A35 G93 V94 V95 Y119 N171 D199 I201 H202 K234 R365 I33 A34 G92 V93 V94 Y118 N170 D198 I200 H201 K233 R364
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009058 biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3b1e, PDBe:3b1e, PDBj:3b1e
PDBsum3b1e
PubMed22674431
UniProtA6BMJ3

[Back to BioLiP]