Structure of PDB 3bm5 Chain B

Receptor sequence
>3bm5B (length=335) Species: 294381 (Entamoeba histolytica HM-1:IMSS) [Search protein sequence]
EQISISSPRKRIYHNILETIGGTPLVELHGVTEHPRIKKGTRILVKLEYF
NPMSSVKDRVGFNIVYQAIKDGRLKPGMEIIESTSGNTGIALCQAGAVFG
YRVNIAMPSTMSVERQMIMKAFGAELILTEGKKGMPGAIEEVNKMIKENP
GKYFVANQFGNPDNTAAHHYTANEIWEDTDGEVDIVVSAVGTSGTVIGVA
EKLKEKKKGIKIIAVEPEESAVLEGKAKGPHGIQGIGAGFIPDIYKKEFV
DEIIPIKTQDAWKMARAVVKYDGIMCGMSSGAAILAGLKEAEKPENEGKT
IVIIVPSCGERYLSTDLYKIKDEGTKIQILDSLLN
3D structure
PDB3bm5 Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: structural evidence for cysteine binding and lack of interactions with serine acetyl transferase.
ChainB
Resolution2.4 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) K58 S280
Catalytic site (residue number reindexed from 1) K57 S279
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 PLP B K58 N88 G192 T193 S194 T196 G236 S280 P307 K57 N87 G191 T192 S193 T195 G235 S279 P306
BS02 CYS B K58 T85 S86 T89 G236 K57 T84 S85 T88 G235 MOAD: Kd=1.1mM
Gene Ontology
Molecular Function
GO:0004124 cysteine synthase activity
Biological Process
GO:0006535 cysteine biosynthetic process from serine
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3bm5, PDBe:3bm5, PDBj:3bm5
PDBsum3bm5
PubMed18350570
UniProtO15570

[Back to BioLiP]