4AOK

Conformational dynamics of aspartate alpha-decarboxylase active site revealed by protein-ligand complexes: 1-methyl-L-aspartate complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004068	molecular_function	aspartate 1-decarboxylase activity
A	0006523	biological_process	alanine biosynthetic process
B	0004068	molecular_function	aspartate 1-decarboxylase activity
B	0006523	biological_process	alanine biosynthetic process
D	0004068	molecular_function	aspartate 1-decarboxylase activity
D	0006523	biological_process	alanine biosynthetic process
E	0004068	molecular_function	aspartate 1-decarboxylase activity
E	0006523	biological_process	alanine biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000269|PubMed:9546220

Chain	Residue	Details
E	3A525
B	3A525

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor

Chain	Residue	Details
B	TYR58
E	TYR58

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
B	THR57
E	THR57
E	GLY73
B	GLY73

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:9546220

Chain	Residue	Details
E	3A525
B	3A525

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 409

Chain	Residue	Details
B	TYR58	activator, increase nucleophilicity, proton acceptor, proton donor
B	3A525	covalently attached, electrofuge, electrophile

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 409

Chain	Residue	Details
E	TYR58	activator, increase nucleophilicity, proton acceptor, proton donor
E	3A525	covalently attached, electrofuge, electrophile

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