Structure of PDB 1gc3 Chain A

Receptor sequence
>1gc3A (length=382) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK
EAARRALAQGKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVGG
SQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGF
VPDPERVRRAITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL
VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPK
EVIKAMASVSRQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRRR
DLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVP
GTDFAAFGHVRLSYATSEENLRKALERFARVL
3D structure
PDB1gc3 Substrate recognition mechanism of thermophilic dual-substrate enzyme.
ChainA
Resolution3.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.1: aspartate transaminase.
2.6.1.78: aspartate--prephenate aminotransferase.
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 TRP A V16 N20 T37 A38 G39 E40 Y322 R361 V16 N20 T37 A38 G39 E40 Y322 R361
BS02 PLP A G100 S101 W125 N175 D203 Y206 K234 R242 G100 S101 W125 N175 D203 Y206 K234 R242
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0033853 aspartate-prephenate aminotransferase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Biological Process
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Cellular Component
External links
PDB RCSB:1gc3, PDBe:1gc3, PDBj:1gc3
PDBsum1gc3
PubMed11432784
UniProtQ56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)

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