Structure of PDB 1gde Chain A

Receptor sequence
>1gdeA (length=388) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
ALSDRLELVSASEIRKLFDIAAGMKDVISLGIGEPDFDTPQHIKEYAKEA
LDKGLTHYGPNIGLLELREAIAEKLKKQNGIEADPKTEIMVLLGANQAFL
MGLSAFLKDGEEVLIPTPAFVSYAPAVILAGGKPVEVPTYEEDEFRLNVD
ELKKYVTDKTRALIINSPCNPTGAVLTKKDLEEIADFVVEHDLIVISDEV
YEHFIYDDARHYSIASLDGMFERTITVNGFSKTFAMTGWRLGFVAAPSWI
IERMVKFQMYNATCPVTFIQYAAAKALKDERSWKAVEEMRKEYDRRRKLV
WKRLNEMGLPTVKPKGAFYIFPRIRDTGLTSKKFSELMLKEARVAVVPGS
AFGKAGEGYVRISYATAYEKLEEAMDRMERVLKERKLV
3D structure
PDB1gde Temperature dependence of the enzyme-substrate recognition mechanism.
ChainA
Resolution1.8 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) K233
Catalytic site (residue number reindexed from 1) K232
Enzyme Commision number 2.6.1.-
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 GLU A F121 N171 R362 F120 N170 R361
BS02 PLP A G95 A96 N97 F121 N167 D199 Y202 S232 K233 R241 G94 A95 N96 F120 N166 D198 Y201 S231 K232 R240
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1gde, PDBe:1gde, PDBj:1gde
PDBsum1gde
PubMed11134972
UniProtO59096

[Back to BioLiP]