Structure of PDB 4y0h Chain D

Receptor sequence
>4y0hD (length=463) Species: 9823 (Sus scrofa) [Search protein sequence]
GFDYDGPLMKTEVPGPRSRELMKQLNIIQNAEAVHFFCNYEESRGNYLVD
VDGNRMLDLYSQISSIPIGYSHPALVKLVQQPQNVSTFINRPALGILPPE
NFVEKLRESLLSVAPKGMSQLITMACGSCSNENAFKTIFMWYRSKERGES
AFSKEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKID
IPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTV
AGIIVEPIQSEGGDNHASDDFFRKLRDISRKHGCAFLVDEVQTGGGSTGK
FWAHEHWGLDDPADVMTFSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPS
KNLLLAEVINIIKREDLLSNAAHAGKVLLTGLLDLQARYPQFISRVRGRG
TFCSFDTPDESIRNKLISIARNKGVMLGGCGDKSIRFRPTLVFRDHHAHL
FLNIFSDILADFK
3D structure
PDB4y0h Mechanism of inactivation of gamma-aminobutyric acid aminotransferase by (1S,3S)-3-amino-4-difluoromethylenyl-1-cyclopentanoic acid (CPP-115)
ChainD
Resolution1.63 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) F189 E265 D298 Q301 K329 T353 R445
Catalytic site (residue number reindexed from 1) F180 E256 D289 Q292 K320 T344 R436
Enzyme Commision number 2.6.1.19: 4-aminobutyrate--2-oxoglutarate transaminase.
2.6.1.22: (S)-3-amino-2-methylpropionate 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 FES D C135 C138 C126 C129
BS02 PLP D C135 G136 S137 F189 H190 E265 D298 V300 Q301 K329 C126 G127 S128 F180 H181 E256 D289 V291 Q292 K320
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0032145 succinate-semialdehyde dehydrogenase binding
GO:0034386 4-aminobutyrate:2-oxoglutarate transaminase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0047298 (S)-3-amino-2-methylpropionate transaminase activity
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009448 gamma-aminobutyric acid metabolic process
GO:0009450 gamma-aminobutyric acid catabolic process
GO:0048148 behavioral response to cocaine
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0005829 cytosol
GO:0032144 4-aminobutyrate transaminase complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4y0h, PDBe:4y0h, PDBj:4y0h
PDBsum4y0h
PubMed25616005
UniProtP80147|GABT_PIG 4-aminobutyrate aminotransferase, mitochondrial (Gene Name=ABAT)

[Back to BioLiP]