5I92

Crystal structure of Glutamate-1-semialdehyde 2,1- aminomutase (GSA) from Pseudomonas aeruginosa

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006779	biological_process	porphyrin-containing compound biosynthetic process
A	0006782	biological_process	protoporphyrinogen IX biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033014	biological_process	tetrapyrrole biosynthetic process
A	0042286	molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity
B	0005737	cellular_component	cytoplasm
B	0006779	biological_process	porphyrin-containing compound biosynthetic process
B	0006782	biological_process	protoporphyrinogen IX biosynthetic process
B	0016853	molecular_function	isomerase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0033014	biological_process	tetrapyrrole biosynthetic process
B	0042286	molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity
C	0005737	cellular_component	cytoplasm
C	0006779	biological_process	porphyrin-containing compound biosynthetic process
C	0006782	biological_process	protoporphyrinogen IX biosynthetic process
C	0016853	molecular_function	isomerase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0033014	biological_process	tetrapyrrole biosynthetic process
C	0042286	molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity
D	0005737	cellular_component	cytoplasm
D	0006779	biological_process	porphyrin-containing compound biosynthetic process
D	0006782	biological_process	protoporphyrinogen IX biosynthetic process
D	0016853	molecular_function	isomerase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0033014	biological_process	tetrapyrrole biosynthetic process
D	0042286	molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity
E	0005737	cellular_component	cytoplasm
E	0006779	biological_process	porphyrin-containing compound biosynthetic process
E	0006782	biological_process	protoporphyrinogen IX biosynthetic process
E	0016853	molecular_function	isomerase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0033014	biological_process	tetrapyrrole biosynthetic process
E	0042286	molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity
F	0005737	cellular_component	cytoplasm
F	0006779	biological_process	porphyrin-containing compound biosynthetic process
F	0006782	biological_process	protoporphyrinogen IX biosynthetic process
F	0016853	molecular_function	isomerase activity
F	0030170	molecular_function	pyridoxal phosphate binding
F	0033014	biological_process	tetrapyrrole biosynthetic process
F	0042286	molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue GOL A 501

Chain	Residue
A	SER114
A	GLY115
A	THR116
A	TYR142
B	SER113
B	GLU117
B	GLY296
B	THR297

---

site_id	AC2
Number of Residues	7
Details	binding site for residue EDO A 502

Chain	Residue
A	GLY356
A	LEU357
A	ALA394
A	GLU399
A	GLY401
A	HOH627
A	ASN211

---

site_id	AC3
Number of Residues	8
Details	binding site for residue EDO B 501

Chain	Residue
B	ASN211
B	PHE355
B	LEU357
B	LEU393
B	ALA394
B	GLU399
B	GLY401
B	HOH666

---

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL C 501

Chain	Residue
C	SER114
C	GLY115
C	THR116
C	TYR142
D	SER113
D	GLU117
D	GLY296
D	THR297
D	HOH604

---

site_id	AC5
Number of Residues	7
Details	binding site for residue EDO C 502

Chain	Residue
C	ASN211
C	PHE355
C	LEU357
C	LEU393
C	ALA394
C	GLY401
C	HOH661

---

site_id	AC6
Number of Residues	3
Details	binding site for residue EDO C 503

Chain	Residue
C	SER84
C	LEU298
C	ASN301

---

site_id	AC7
Number of Residues	7
Details	binding site for residue EDO D 501

Chain	Residue
D	ASN211
D	PHE355
D	LEU357
D	LEU393
D	ALA394
D	GLY401
D	HOH659

---

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO D 502

Chain	Residue
C	HOH631
D	SER114
D	GLY115
D	THR116
D	TYR142
D	HOH736
D	HOH862

---

site_id	AC9
Number of Residues	7
Details	binding site for residue EDO E 501

Chain	Residue
E	ASN211
E	PHE355
E	LEU357
E	LEU393
E	ALA394
E	GLY401
E	HOH654

---

site_id	AD1
Number of Residues	7
Details	binding site for residue LEU F 501

Chain	Residue
F	ARG381
F	ALA422
F	PHE423
F	ALA424
F	ALA425
F	HOH643
F	HOH894

---

site_id	AD2
Number of Residues	7
Details	binding site for residue EDO F 502

Chain	Residue
F	ASN211
F	PHE355
F	LEU357
F	LEU393
F	ALA394
F	GLY401
F	HOH647

---

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO F 503

Chain	Residue
F	GLU139
F	THR178
F	LEU179
F	PRO180
F	HOH635
F	HOH695

---

site_id	AD4
Number of Residues	2
Details	binding site for residue EDO F 504

Chain	Residue
F	LYS27
F	HOH843

---

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	37
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVmt.GF.RvAlggaqayygvtp....DLStfGKiigGG

Chain	Residue	Details
A	LEU234-GLY270

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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