4UOX

Crystal structure of YgjG in complex with Pyridoxal-5'-phosphate and putrescine

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	0016740	molecular_function	transferase activity
A	0019161	molecular_function	diamine transaminase activity
A	0019477	biological_process	L-lysine catabolic process
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	0016740	molecular_function	transferase activity
B	0019161	molecular_function	diamine transaminase activity
B	0019477	biological_process	L-lysine catabolic process
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	0016740	molecular_function	transferase activity
C	0019161	molecular_function	diamine transaminase activity
C	0019477	biological_process	L-lysine catabolic process
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	0016740	molecular_function	transferase activity
D	0019161	molecular_function	diamine transaminase activity
D	0019477	biological_process	L-lysine catabolic process
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PLP C 800

Chain	Residue
C	SER149
C	VAL273
C	GLN274
C	LYS300
C	PUT801
C	HOH2053
C	HOH2070
C	HOH2090
C	HOH2105
D	THR331
D	THR332
C	GLY150
C	THR151
C	PHE180
C	HIS181
C	GLY182
C	GLU238
C	GLU243
C	ASP271

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PUT C 801

Chain	Residue
C	GLU243
C	LYS300
C	PLP800
D	GLN119
D	THR332

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP D 800

Chain	Residue
C	THR331
C	THR332
C	HOH2052
C	HOH2055
D	GLY150
D	THR151
D	PHE180
D	HIS181
D	GLU238
D	GLU243
D	ASP271
D	VAL273
D	GLN274
D	LYS300
D	HOH2041
D	HOH2059
D	HOH2081

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT A 1460

Chain	Residue
A	GLU316
B	GLU44

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT C 1459

Chain	Residue
B	PHE207
B	ARG208
C	GLY206
C	PHE207
C	ARG208
C	FMT1460

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT C 1460

Chain	Residue
B	GLY206
C	PRO205
C	GLY206
C	FMT1459

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 1461

Chain	Residue
A	GLY49
A	GLU52
A	TYR53

---

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT D 1462

Chain	Residue
D	HOH2124

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT D 1460

Chain	Residue
A	ARG208
D	GLY206
D	PHE207
D	ARG208

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1460

Chain	Residue
B	GLN358
B	LYS362
B	THR432
B	HOH2137
D	PRO251

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1462

Chain	Residue
A	LYS43
A	GLU44
B	TYR143
B	GLU316
C	LYS443

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1461

Chain	Residue
C	ARG3
C	LEU328
C	HOH2101
D	THR195
D	LYS198
D	PRO199

---

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 1461

Chain	Residue
B	MET201
B	HOH2065
C	PHE171
D	MET201

---

site_id	BC5
Number of Residues	19
Details	Binding site for residues PLP A 800 and PUT A 801

Chain	Residue
B	THR332
A	SER149
A	GLY150
A	THR151
A	PHE180
A	HIS181
A	GLY182
A	GLU238
A	GLU243
A	ASP271
A	VAL273
A	GLN274
A	LYS300
A	HOH2051
A	HOH2070
A	HOH2145
A	HOH2146
B	GLN119
B	THR331

---

site_id	BC6
Number of Residues	19
Details	Binding site for residues PLP B 800 and PUT B 801

Chain	Residue
A	GLN119
A	THR331
A	THR332
A	HOH2123
A	HOH2124
B	SER149
B	GLY150
B	THR151
B	PHE180
B	HIS181
B	GLU238
B	GLU243
B	ASP271
B	VAL273
B	GLN274
B	LYS300
B	LEU419
B	HOH2041
B	HOH2089

---

Functional Information from PROSITE/UniProt

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	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25423189","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25423189","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"25423189","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UOY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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