Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4A0G

Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana in its apo form.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
A	0004141	molecular_function	dethiobiotin synthase activity
A	0005524	molecular_function	ATP binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0008483	molecular_function	transaminase activity
A	0009102	biological_process	biotin biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016874	molecular_function	ligase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
B	0004141	molecular_function	dethiobiotin synthase activity
B	0005524	molecular_function	ATP binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0008483	molecular_function	transaminase activity
B	0009102	biological_process	biotin biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016874	molecular_function	ligase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
C	0004141	molecular_function	dethiobiotin synthase activity
C	0005524	molecular_function	ATP binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0008483	molecular_function	transaminase activity
C	0009102	biological_process	biotin biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016874	molecular_function	ligase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
D	0004141	molecular_function	dethiobiotin synthase activity
D	0005524	molecular_function	ATP binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0008483	molecular_function	transaminase activity
D	0009102	biological_process	biotin biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016874	molecular_function	ligase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP A 1644

Chain	Residue
A	ASN430
A	PHE618
A	LYS644
A	HOH2136
A	HOH2137
A	HOH2159
A	HOH2185
B	HIS679
B	SER680
A	GLY431
A	SER432
A	TYR473
A	HIS474
A	GLY475
A	GLU581
A	ASP615
A	VAL617

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 1644

Chain	Residue
A	HIS679
A	SER680
A	HOH2125
A	HOH2164
A	HOH2165
A	HOH2166
B	ASN430
B	GLY431
B	SER432
B	TYR473
B	HIS474
B	GLU581
B	ASP615
B	VAL617
B	PHE618
B	LYS644
B	HOH2098

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP C 1644

Chain	Residue
C	ASN430
C	GLY431
C	SER432
C	ILE435
C	TYR473
C	HIS474
C	GLU581
C	ASP615
C	VAL617
C	PHE618
C	LYS644
D	HIS679
D	SER680

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP D 1644

Chain	Residue
C	HIS679
C	SER680
D	ASN430
D	GLY431
D	SER432
D	ILE435
D	TYR473
D	GLU581
D	ASP615
D	VAL617
D	PHE618
D	LYS644
D	HOH2055

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1812

Chain	Residue
A	THR24
A	LYS28
A	LYS55
A	GLY191
A	SO41814

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1812

Chain	Residue
A	SER195
A	PRO196
B	GLY223
B	GLY224
B	ILE225
B	SER226
B	HOH2041

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1813

Chain	Residue
A	GLY223
A	GLY224
A	ILE225
A	SER226
B	SER195
B	PRO196

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1813

Chain	Residue
B	LYS28
B	LYS55
B	ASP66
B	GLU188
B	ALA190
B	GLY191
B	MG1814

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 1807

Chain	Residue
C	THR24
C	LYS28
C	LYS55
C	ALA190
C	GLY191
C	SO41809
C	HOH2005

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 1808

Chain	Residue
C	SER143
C	SER195
C	PRO196
D	GLY223
D	GLY224
D	ILE225
D	SER226

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 1808

Chain	Residue
C	GLY223
C	GLY224
C	ILE225
C	SER226
D	SER143
D	SER195
D	PRO196

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 1809

Chain	Residue
D	THR24
D	LYS28
D	LYS55
D	GLY191
D	MG1810
D	HOH2005

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1814

Chain	Residue
A	SER25
A	GLY27
A	LYS28
A	THR29
A	SO41812

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 1809

Chain	Residue
C	SER25
C	LEU26
C	GLY27
C	LYS28
C	THR29
C	LEU30
C	SO41807

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1814

Chain	Residue
B	LYS28
B	THR29
B	ASP66
B	GLU188
B	SO41813
B	HOH2004

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1810

Chain	Residue
D	THR29
D	ASP66
D	GLU188
D	SO41809
D	HOH2005

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIfDEVft.GFwRlGvetttellgckp....DIAcfAKlltGG

Chain	Residue	Details
A	VAL612-GLY649

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	47
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P13000","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0G","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Site: {"description":"Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM","evidences":[{"source":"UniProtKB","id":"P12995","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"22547782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A0R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)