Structure of PDB 4w5k Chain A

Receptor sequence
>4w5kA (length=380) [Search protein sequence]
GLGQDFRMDPAKRKVNLSIGVYRDDADQPFVLECVKQATLGTNMDYAPVT
GIASFVEEAQKLCFGPTCAALRDGRIASCQTLGGTGALRIGGDLLNRFVA
NCNRIYGPDVGYPNHESIFAKAGMELTPYSYYDPATKGLNLAGMLECLDK
APEGSVILVHACAHNPTGVDPTHDDWRQVCDVIKRRNHIPFVDMAYQGFA
TGQLDYDAFVPRHLVDMVPNLIVAQSFSANFGLYGHRCGALHISTASAEE
AKRLVSQLALLIRPMYSNPPLYGAWVVSSILKDPQLTALWKKELKQMSSR
IAEVRKRLVSELKACGSVHDWSHIERQVGMMAYTGLTREQVELLRSEYHI
YMTLNGRAAVSGLNSTNVEYVSQAIHNVTK
3D structure
PDB4w5k Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.
ChainA
Resolution1.7 Å
3D
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
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 G91 G92 T93 Y120 N173 D201 A203 Y204 S234 S236 R245 G83 G84 T85 Y112 N165 D193 A195 Y196 S226 S228 R237
Gene Ontology
Molecular Function
GO:0004021 L-alanine:2-oxoglutarate aminotransferase 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
GO:0019509 L-methionine salvage from methylthioadenosine
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0031981 nuclear lumen
GO:0097014 ciliary plasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4w5k, PDBe:4w5k, PDBj:4w5k
PDBsum4w5k
PubMed25945710
UniProtQ385Q9

[Back to BioLiP]