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Structure of PDB 1gc3 Chain H Binding Site BS02

Receptor Information >1gc3 Chain H (length=382) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK EAARRALAQGKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVGG SQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGF VPDPERVRRAITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPK EVIKAMASVSRQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRRR DLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVP GTDFAAFGHVRLSYATSEENLRKALERFARVL

Ligand information Ligand ID PLP InChI InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14) InChIKey NGVDGCNFYWLIFO-UHFFFAOYSA-N SMILES Software SMILES CACTVS 3.341 Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O OpenEye OEToolkits 1.5.0 Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O ACDLabs 10.04 O=P(O)(O)OCc1cnc(c(O)c1C=O)C Formula C8 H10 N O6 P Name PYRIDOXAL-5'-PHOSPHATE; VITAMIN B6 Phosphate ChEMBL CHEMBL82202 DrugBank DB00114 ZINC ZINC000001532514 PDB chain 1gc3 Chain H Residue 3913 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1gc3 Substrate recognition mechanism of thermophilic dual-substrate enzyme. Resolution 3.3 Å Binding residue (original residue number in PDB) G3600 S3601 W3625 N3675 D3703 Y3706 K3734 R3742 Binding residue (residue number reindexed from 1) G100 S101 W125 N175 D203 Y206 K234 R242 Annotation score 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.

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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