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Structure of PDB 1gc3 Chain H

Receptor sequence >1gc3H (length=382) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence] MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK EAARRALAQGKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVGG SQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGF VPDPERVRRAITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPK EVIKAMASVSRQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRRR DLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVP GTDFAAFGHVRLSYATSEENLRKALERFARVL

3D structure PDB 1gc3 Substrate recognition mechanism of thermophilic dual-substrate enzyme. Chain H Resolution 3.3 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) W3625 D3703 I3705 K3734 Catalytic site (residue number reindexed from 1) W125 D203 I205 K234 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 H V3516 G3539 N3675 Y3822 R3861 V16 G39 N175 Y322 R361 BS02 PLP H G3600 S3601 W3625 N3675 D3703 Y3706 K3734 R3742 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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