Structure of PDB 1b5p Chain B Binding Site BS01
Receptor Information
>1b5p Chain B (length=382) Species:
300852
(Thermus thermophilus HB8) [
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MRGLSRRVQAMKPSATVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK
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
1b5p Chain B Residue 413 [
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Receptor-Ligand Complex Structure
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PDB
1b5p
Substrate recognition mechanism of thermophilic dual-substrate enzyme
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
G99 G100 S101 W125 N175 D203 I205 Y206 A233 K234 R242
Binding residue
(residue number reindexed from 1)
G99 G100 S101 W125 N175 D203 I205 Y206 A233 K234 R242
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
W125 D203 I205 K234
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1b5p
,
PDBe:1b5p
,
PDBj:1b5p
PDBsum
1b5p
PubMed
11432784
UniProt
Q56232
|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)
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