Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5H7D

Crystal structure of the YgjG-protein A-Zpa963-calmodulin complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0008483	molecular_function	transaminase activity
A	0009447	biological_process	putrescine catabolic process
A	0019161	molecular_function	diamine transaminase activity
A	0019477	biological_process	L-lysine catabolic process
A	0019865	molecular_function	immunoglobulin binding
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033094	molecular_function	putrescine--2-oxoglutarate transaminase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
B	0005829	cellular_component	cytosol
B	0008483	molecular_function	transaminase activity
B	0009447	biological_process	putrescine catabolic process
B	0019161	molecular_function	diamine transaminase activity
B	0019477	biological_process	L-lysine catabolic process
B	0019865	molecular_function	immunoglobulin binding
B	0030170	molecular_function	pyridoxal phosphate binding
B	0033094	molecular_function	putrescine--2-oxoglutarate transaminase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
C	0005829	cellular_component	cytosol
C	0008483	molecular_function	transaminase activity
C	0009447	biological_process	putrescine catabolic process
C	0019161	molecular_function	diamine transaminase activity
C	0019477	biological_process	L-lysine catabolic process
C	0019865	molecular_function	immunoglobulin binding
C	0030170	molecular_function	pyridoxal phosphate binding
C	0033094	molecular_function	putrescine--2-oxoglutarate transaminase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
D	0005829	cellular_component	cytosol
D	0008483	molecular_function	transaminase activity
D	0009447	biological_process	putrescine catabolic process
D	0019161	molecular_function	diamine transaminase activity
D	0019477	biological_process	L-lysine catabolic process
D	0019865	molecular_function	immunoglobulin binding
D	0030170	molecular_function	pyridoxal phosphate binding
D	0033094	molecular_function	putrescine--2-oxoglutarate transaminase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
E	0005509	molecular_function	calcium ion binding
E	0019865	molecular_function	immunoglobulin binding
F	0005509	molecular_function	calcium ion binding
F	0019865	molecular_function	immunoglobulin binding
G	0005509	molecular_function	calcium ion binding
G	0019865	molecular_function	immunoglobulin binding
H	0005509	molecular_function	calcium ion binding
H	0019865	molecular_function	immunoglobulin binding
I	0005829	cellular_component	cytosol
I	0008483	molecular_function	transaminase activity
I	0009447	biological_process	putrescine catabolic process
I	0019161	molecular_function	diamine transaminase activity
I	0019477	biological_process	L-lysine catabolic process
I	0019865	molecular_function	immunoglobulin binding
I	0030170	molecular_function	pyridoxal phosphate binding
I	0033094	molecular_function	putrescine--2-oxoglutarate transaminase activity
I	0042802	molecular_function	identical protein binding
I	0042803	molecular_function	protein homodimerization activity
J	0005829	cellular_component	cytosol
J	0008483	molecular_function	transaminase activity
J	0009447	biological_process	putrescine catabolic process
J	0019161	molecular_function	diamine transaminase activity
J	0019477	biological_process	L-lysine catabolic process
J	0019865	molecular_function	immunoglobulin binding
J	0030170	molecular_function	pyridoxal phosphate binding
J	0033094	molecular_function	putrescine--2-oxoglutarate transaminase activity
J	0042802	molecular_function	identical protein binding
J	0042803	molecular_function	protein homodimerization activity
K	0005509	molecular_function	calcium ion binding
K	0019865	molecular_function	immunoglobulin binding
L	0005509	molecular_function	calcium ion binding
L	0019865	molecular_function	immunoglobulin binding
M	0005829	cellular_component	cytosol
M	0008483	molecular_function	transaminase activity
M	0009447	biological_process	putrescine catabolic process
M	0019161	molecular_function	diamine transaminase activity
M	0019477	biological_process	L-lysine catabolic process
M	0019865	molecular_function	immunoglobulin binding
M	0030170	molecular_function	pyridoxal phosphate binding
M	0033094	molecular_function	putrescine--2-oxoglutarate transaminase activity
M	0042802	molecular_function	identical protein binding
M	0042803	molecular_function	protein homodimerization activity
N	0005829	cellular_component	cytosol
N	0008483	molecular_function	transaminase activity
N	0009447	biological_process	putrescine catabolic process
N	0019161	molecular_function	diamine transaminase activity
N	0019477	biological_process	L-lysine catabolic process
N	0019865	molecular_function	immunoglobulin binding
N	0030170	molecular_function	pyridoxal phosphate binding
N	0033094	molecular_function	putrescine--2-oxoglutarate transaminase activity
N	0042802	molecular_function	identical protein binding
N	0042803	molecular_function	protein homodimerization activity
O	0005509	molecular_function	calcium ion binding
O	0019865	molecular_function	immunoglobulin binding
P	0005509	molecular_function	calcium ion binding
P	0019865	molecular_function	immunoglobulin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CA E 501

Chain	Residue
E	ASP165
E	ASP167
E	ASP169
E	THR171
E	GLU176

site_id	AC2
Number of Residues	5
Details	binding site for residue CA E 502

Chain	Residue
E	GLU212
E	ASP201
E	ASP203
E	ASN205
E	THR207

site_id	AC3
Number of Residues	5
Details	binding site for residue CA F 501

Chain	Residue
F	ASP165
F	ASP167
F	ASP169
F	THR171
F	GLU176

site_id	AC4
Number of Residues	5
Details	binding site for residue CA F 502

Chain	Residue
F	ASP201
F	ASP203
F	ASN205
F	THR207
F	GLU212

site_id	AC5
Number of Residues	5
Details	binding site for residue CA G 501

Chain	Residue
G	ASP165
G	ASP167
G	ASP169
G	THR171
G	GLU176

site_id	AC6
Number of Residues	5
Details	binding site for residue CA G 502

Chain	Residue
G	ASP201
G	ASP203
G	ASN205
G	THR207
G	GLU212

site_id	AC7
Number of Residues	5
Details	binding site for residue CA H 501

Chain	Residue
H	ASP165
H	ASP167
H	ASP169
H	THR171
H	GLU176

site_id	AC8
Number of Residues	5
Details	binding site for residue CA H 502

Chain	Residue
H	ASP201
H	ASP203
H	ASN205
H	THR207
H	GLU212

site_id	AC9
Number of Residues	5
Details	binding site for residue CA K 501

Chain	Residue
K	ASP165
K	ASP167
K	ASP169
K	THR171
K	GLU176

site_id	AD1
Number of Residues	5
Details	binding site for residue CA K 502

Chain	Residue
K	ASP201
K	ASP203
K	ASN205
K	THR207
K	GLU212

site_id	AD2
Number of Residues	5
Details	binding site for residue CA L 501

Chain	Residue
L	ASP165
L	ASP167
L	ASP169
L	THR171
L	GLU176

site_id	AD3
Number of Residues	5
Details	binding site for residue CA L 502

Chain	Residue
L	ASP201
L	ASP203
L	ASN205
L	THR207
L	GLU212

site_id	AD4
Number of Residues	5
Details	binding site for residue CA O 501

Chain	Residue
O	ASP165
O	ASP167
O	ASP169
O	THR171
O	GLU176

site_id	AD5
Number of Residues	5
Details	binding site for residue CA O 502

Chain	Residue
O	ASP201
O	ASP203
O	ASN205
O	THR207
O	GLU212

site_id	AD6
Number of Residues	5
Details	binding site for residue CA P 501

Chain	Residue
P	ASP165
P	ASP167
P	ASP169
P	THR171
P	GLU176

site_id	AD7
Number of Residues	5
Details	binding site for residue CA P 502

Chain	Residue
P	ASP201
P	ASP203
P	ASN205
P	THR207
P	GLU212

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL

Chain	Residue	Details
E	ASP165-LEU177
E	ASP201-PHE213

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. MIlDEVqt.GMgRtGkmfacehenvqp....DILclAKalgGG

Chain	Residue	Details
A	MET268-GLY305

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00448

Chain	Residue	Details
E	ASP165
E	GLU212
F	ASP165
F	ASP167
F	ASP169
F	THR171
F	GLU176
F	ASP201
F	ASP203
F	ASN205
F	THR207
E	ASP167
F	GLU212
G	ASP165
G	ASP167
G	ASP169
G	THR171
G	GLU176
G	ASP201
G	ASP203
G	ASN205
G	THR207
E	ASP169
G	GLU212
H	ASP165
H	ASP167
H	ASP169
H	THR171
H	GLU176
H	ASP201
H	ASP203
H	ASN205
H	THR207
E	THR171
H	GLU212
K	ASP165
K	ASP167
K	ASP169
K	THR171
K	GLU176
K	ASP201
K	ASP203
K	ASN205
K	THR207
E	GLU176
K	GLU212
L	ASP165
L	ASP167
L	ASP169
L	THR171
L	GLU176
L	ASP201
L	ASP203
L	ASN205
L	THR207
E	ASP201
L	GLU212
O	ASP165
O	ASP167
O	ASP169
O	THR171
O	GLU176
O	ASP201
O	ASP203
O	ASN205
O	THR207
E	ASP203
O	GLU212
P	ASP165
P	ASP167
P	ASP169
P	THR171
P	GLU176
P	ASP201
P	ASP203
P	ASN205
P	THR207
E	ASN205
P	GLU212
E	THR207

site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: N-acetylalanine => ECO:0000250

Chain	Residue	Details
E	ALA146
F	ALA146
G	ALA146
H	ALA146
K	ALA146
L	ALA146
O	ALA146
P	ALA146

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:25423189, ECO:0007744\|PDB:4UOY

Chain	Residue	Details
A	LYS300
B	LYS300
C	LYS300
D	LYS300
I	LYS300
J	LYS300
M	LYS300
N	LYS300

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