Structure of PDB 1o4s Chain A

Receptor sequence
>1o4sA (length=375) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VSRRISEIPISKTMELDAKAKALIKKGEDVINLTAGEPDFPTPEPVVEEA
VRFLQKGEVKYTDPRGIYELREGIAKRIGERYKKDISPDQVVVTNGAKQA
LFNAFMALLDPGDEVIVFSPVWVSYIPQIILAGGTVNVVETFMSKNFQPS
LEEVEGLLVGKTKAVLINSPNNPTGVVYRREFLEGLVRLAKKRNFYIISD
EVYDSLVYTDEFTSILDVSEGFDRIVYINGFSKSHSMTGWRVGYLISSEK
VATAVSKIQSHTTSCINTVAQYAALKALEVDNSYMVQTFKERKNFVVERL
KKMGVKFVEPEGAFYLFFKVRGDDVKFCERLLEEKKVALVPGSAFLKPGF
VRLSFATSIERLTEALDRIEDFLNS
3D structure
PDB1o4s Crystal structure of an aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 A resolution
ChainA
Resolution1.9 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) W123 D201 V203 K234
Catalytic site (residue number reindexed from 1) W122 D200 V202 K233
Enzyme Commision number 2.6.1.1: aspartate transaminase.
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 G97 A98 K99 W123 N169 N173 D201 V203 Y204 S233 K234 R242 G96 A97 K98 W122 N168 N172 D200 V202 Y203 S232 K233 R241
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1o4s, PDBe:1o4s, PDBj:1o4s
PDBsum1o4s
PubMed15103638
UniProtQ9X0Y2|AAT_THEMA Aspartate aminotransferase (Gene Name=aspC)

[Back to BioLiP]