1KNP

E. coli L-aspartate oxidase: mutant R386L in complex with succinate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008734	molecular_function	L-aspartate oxidase activity
A	0009435	biological_process	NAD+ biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0034628	biological_process	'de novo' NAD+ biosynthetic process from L-aspartate
A	0044281	biological_process	small molecule metabolic process
A	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 541

Chain	Residue
A	THR353
A	GLY355
A	GLU375
A	SER377
A	HOH812

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site_id	AC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD A 800

Chain	Residue
A	ALA19
A	SER37
A	LYS38
A	SER45
A	THR46
A	TYR48
A	ALA49
A	GLN50
A	GLY51
A	GLY52
A	THR160
A	ASN161
A	ALA162
A	ALA203
A	THR204
A	GLY205
A	ASN216
A	ASP223
A	LEU257
A	HIS351
A	TYR352
A	GLY374
A	GLU375
A	SER389
A	SER391
A	LEU392
A	CYS395
A	SIN801
A	GLY15
A	SER16
A	GLY17
A	ALA18

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site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SIN A 801

Chain	Residue
A	GLY51
A	GLU121
A	HIS244
A	THR259
A	GLU260
A	ARG290
A	HIS351
A	ALA388
A	SER389
A	SER391
A	FAD800

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:11294641, ECO:0000305|PubMed:11863440, ECO:0007744|PDB:1KNP

Chain	Residue	Details
A	ARG290

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site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:11863440, ECO:0007744|PDB:1KNP, ECO:0007744|PDB:1KNR

Chain	Residue	Details
A	SER16
A	LYS38
A	SER45
A	ASN161
A	ASP223
A	GLU375
A	SER391

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:11863440, ECO:0007744|PDB:1KNP

Chain	Residue	Details
A	HIS244
A	THR259
A	SER389

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Important in orienting the L-aspartate substrate => ECO:0000305|PubMed:11294641

Chain	Residue	Details
A	GLU121

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 11863440

Chain	Residue	Details
A	LEU386
A	ARG290
A	HIS351

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 739

Chain	Residue	Details
A	GLU121	electrostatic stabiliser, proton acceptor, steric role
A	HIS244	electrostatic stabiliser
A	ARG290	electrostatic stabiliser, proton acceptor, proton donor
A	HIS351	electrostatic stabiliser
A	LEU386	electrostatic stabiliser

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