4E77

2.0A Crystal Structure of a Glutamate-1-Semialdehyde Aminotransferase from Yersinia pestis CO92

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	0008483	molecular_function	transaminase activity
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA A 501

Chain	Residue
A	ASP329
A	GLU388
A	HOH646
A	HOH679
A	HOH778
A	HOH876
A	HOH932

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NO3 A 502

Chain	Residue
A	VAL239
A	GLY264
A	LYS265
A	VAL273
A	HOH730
A	HOH905
A	SER114
A	GLY115

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Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	37
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIiDEVmt.GF.RvAlagaqdyyhvip....DLTclGKiigGG

Chain	Residue	Details
A	LEU234-GLY270

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00375

Chain	Residue	Details
A	LYS265

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