Structure of PDB 1gde Chain B

Receptor sequence
>1gdeB (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.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 GLU B G534 F621 N671 Y820 G33 F120 N170 Y319
BS02 PLP B G595 A596 N597 F621 N667 D699 Y702 S732 K733 R741 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1gde, PDBe:1gde, PDBj:1gde
PDBsum1gde
PubMed11134972
UniProtO59096

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