Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DTY

CRYSTAL STRUCTURE OF ADENOSYLMETHIONINE-8-AMINO-7-OXONANOATE AMINOTRANSFERASE WITH PYRIDOXAL PHOSPHATE COFACTOR.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
A	0005737	cellular_component	cytoplasm
A	0008483	molecular_function	transaminase activity
A	0009102	biological_process	biotin biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042803	molecular_function	protein homodimerization activity
B	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
B	0005737	cellular_component	cytoplasm
B	0008483	molecular_function	transaminase activity
B	0009102	biological_process	biotin biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 471

Chain	Residue
A	VAL96
A	THR99
A	PRO100
A	LEU103

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 472

Chain	Residue
A	SER297
A	ASP298
B	THR21

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA B 475

Chain	Residue
B	PRO100
B	LEU103
B	VAL96
B	THR99

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 476

Chain	Residue
A	SER19
A	THR21
B	SER297
B	ASP298
B	GLY302

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP A 450

Chain	Residue
A	SER111
A	GLY112
A	SER113
A	TYR144
A	HIS145
A	GLY146
A	GLU211
A	ASP245
A	ILE247
A	ALA248
A	LYS274
A	HOH1145
A	HOH1146
A	HOH1166
B	PRO308
B	THR309

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP B 450

Chain	Residue
A	THR309
B	GLY112
B	SER113
B	TYR144
B	HIS145
B	GLU211
B	ASP245
B	ALA248
B	LYS274
B	HOH1008
B	HOH1030
B	HOH1272

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEIat.GFgRtGklfacehaeiap....DILclGKaltGG

Chain	Residue	Details
A	LEU242-GLY279

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10452893","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12218056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MLY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJ3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10452893","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12379100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14756557","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DTY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MGV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S07","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10452893","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10452893","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12379100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14756557","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MGV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S07","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10452893","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QJ3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10452893","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12218056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MLY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MLZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJ3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Site: {"description":"Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"12379100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14756557","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DTY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MGV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S09","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S0A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	ASP245
A	TYR144

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	ASP245
B	TYR144

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	ASP245
A	LYS274
A	TYR144

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	ASP245
B	LYS274
B	TYR144

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	ASP245
A	LYS274
A	TYR168

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	ASP245
B	LYS274
B	TYR168

site_id	MCSA1
Number of Residues	4
Details	M-CSA 249

Chain	Residue	Details
A	TYR17	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role
A	TYR144	hydrogen bond acceptor, steric role, van der waals interaction
A	ASP245	electrostatic stabiliser, hydrogen bond acceptor, increase basicity, steric role
A	LYS274	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 249

Chain	Residue	Details
B	TYR17	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, steric role
B	TYR144	hydrogen bond acceptor, steric role, van der waals interaction
B	ASP245	electrostatic stabiliser, hydrogen bond acceptor, increase basicity, steric role
B	LYS274	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)