Structure of PDB 2ctz Chain B

Receptor sequence
>2ctzB (length=421) Species: 274 (Thermus thermophilus) [Search protein sequence]
MRFETLQLHAGYEPEPTTLSRQVPIYPTTSYVFKSPEHAANLFALKEFGN
IYSRIMNPTVDVLEKRLAALEGGKAALATASGHAAQFLALTTLAQAGDNI
VSTPNLYGGTFNQFKVTLKRLGIEVRFTSREERPEEFLALTDEKTRAWWV
ESIGNPALNIPDLEALAQAAREKGVALIVDNTFGMGGYLLRPLAWGAALV
THSLTKWVGGHGAVIAGAIVDGGNFPWEGGRYPLLTEPQPGYHGLRLTEA
FGELAFIVKARVDGLRDQGQALGPFEAWVVLLGMETLSLRAERHVENTLH
LAHWLLEQPQVAWVNYPGLPHHPHHDRAQKYFKGKPGAVLTFGLKGGYEA
AKRFISRLKLISHLANVGDTRTLAIHPASTTHSQLSPEEQAQAGVSPEMV
RLSVGLEHVEDLKAELKEALA
3D structure
PDB2ctz Crystal structure of o-acetyl homoserine sulfhydrylase from Thermus thermophilus HB8
ChainB
Resolution2.6 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) R54 Y107 D180 K206
Catalytic site (residue number reindexed from 1) R54 Y107 D180 K206
Enzyme Commision number 2.5.1.-
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 G82 H83 Q86 Y107 D180 T182 F183 S203 T205 K206 G82 H83 Q86 Y107 D180 T182 F183 S203 T205 K206
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
GO:0030170 pyridoxal phosphate binding
GO:0051009 O-acetylhomoserine sulfhydrylase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0009086 methionine biosynthetic process
GO:0019346 transsulfuration

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2ctz, PDBe:2ctz, PDBj:2ctz
PDBsum2ctz
PubMed
UniProtQ5SK88|METY1_THET8 O-acetyl-L-homoserine sulfhydrylase 1 (Gene Name=oah1)

[Back to BioLiP]