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BioLiP

Structure of PDB 1gc4 Chain D Binding Site BS02

Receptor Information

>1gc4 Chain D (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

ASP

InChI

InChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1

InChIKey

CKLJMWTZIZZHCS-REOHCLBHSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.7.0	C(C(C(=O)O)N)C(=O)O
OpenEye OEToolkits 1.7.0	C([C@@H](C(=O)O)N)C(=O)O
CACTVS 3.370	N[CH](CC(O)=O)C(O)=O
CACTVS 3.370	N[C@@H](CC(O)=O)C(O)=O
ACDLabs 12.01	O=C(O)CC(N)C(=O)O

Formula

C4 H7 N O4

Name

ASPARTIC ACID

PDB chain

1gc4 Chain D Residue 1914 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1gc4 Substrate recognition mechanism of thermophilic dual-substrate enzyme.
Resolution	3.3 Å
Binding residue (original residue number in PDB)	N1675 Y1822 R1861
Binding residue (residue number reindexed from 1)	N175 Y322 R361
Annotation score	5

Enzymatic activity

Catalytic site (original residue number in PDB)	W1625 D1703 I1705 K1734
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:1gc4, PDBe:1gc4, PDBj:1gc4
PDBsum	1gc4
PubMed	11432784
UniProt	Q56232\|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)

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