Structure of PDB 2cb1 Chain A

Receptor sequence
>2cb1A (length=404) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MEYTTLAVLAGLPEDPHGAVGLPIYAVAAYGFKTLEEGQERFATGEGYVY
ARQKDPTAKALEERLKALEGALEAVVLASGQAATFAALLALLRPGDEVVA
AKGLFGQTIGLFGQVLSLMGVTVRYVDPEPEAVREALSAKTRAVFVETVA
NPALLVPDLEALATLAEEAGVALVVDNTFGAAGALCRPLAWGAHVVVESL
TKWASGHGSVLGGAVLSRETELWRNYPQFLQPWEALRARCFPERVRTLGL
SLCGMALSPFNAYLLFQGLETVALRVARMSETARFLAERLQGHPKVKALR
YPGLPEDPAHRNARKYLASGGPILTLDLGDLERASRFLGAIRLLKAANLG
DARTLLVHPWTTTHSRLKEEARLQAGVTPGLVRVSVGLEDPLDLLALFEE
ALEA
3D structure
PDB2cb1 The Crystal Structure of O-Acetyl Homoserine Sulfhydrylase
ChainA
Resolution2.0 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) R52 F105 D176 K202
Catalytic site (residue number reindexed from 1) R52 F105 D176 K202
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 A S79 G80 Q81 F105 D176 T178 S199 T201 K202 A411 S79 G80 Q81 F105 D176 T178 S199 T201 K202 A404
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:2cb1, PDBe:2cb1, PDBj:2cb1
PDBsum2cb1
PubMed
UniProtQ5SJ58|METY2_THET8 O-acetyl-L-homoserine sulfhydrylase 2 (Gene Name=oah2)

[Back to BioLiP]