Structure of PDB 1gd9 Chain B

Receptor sequence
>1gd9B (length=388) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
ALSDRLELVSASEIRKLFDIAAGMKDVISLGIGEPDFDTPQHIKEYAKEA
LDKGLTHYGPNIGLLELREAIAEKLKKQNGIEADPKTEIMVLLGANQAFL
MGLSAFLKDGEEVLIPTPAFVSYAPAVILAGGKPVEVPTYEEDEFRLNVD
ELKKYVTDKTRALIINSPCNPTGAVLTKKDLEEIADFVVEHDLIVISDEV
YEHFIYDDARHYSIASLDGMFERTITVNGFSKTFAMTGWRLGFVAAPSWI
IERMVKFQMYNATCPVTFIQYAAAKALKDERSWKAVEEMRKEYDRRRKLV
WKRLNEMGLPTVKPKGAFYIFPRIRDTGLTSKKFSELMLKEARVAVVPGS
AFGKAGEGYVRISYATAYEKLEEAMDRMERVLKERKLV
3D structure
PDB1gd9 Temperature dependence of the enzyme-substrate recognition mechanism.
ChainB
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) F621 D699 V701 K733
Catalytic site (residue number reindexed from 1) F120 D198 V200 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 PLP B G595 A596 N597 F621 N671 D699 V701 Y702 S732 K733 R741 G94 A95 N96 F120 N170 D198 V200 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:1gd9, PDBe:1gd9, PDBj:1gd9
PDBsum1gd9
PubMed11134972
UniProtO59096

[Back to BioLiP]