2HUF

Crystal structure of Aedes aegypti alanine glyoxylate aminotransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005777	cellular_component	peroxisome
A	0008453	molecular_function	alanine-glyoxylate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0009436	biological_process	glyoxylate catabolic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0005777	cellular_component	peroxisome
B	0008453	molecular_function	alanine-glyoxylate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009436	biological_process	glyoxylate catabolic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 1BO B 601

Chain	Residue
A	HIS45
B	PRO25
B	SER155
B	LEU347
B	ARG356
B	HOH816

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1BO A 602

Chain	Residue
B	HIS45
B	TYR257
A	SER155
A	ARG356
A	HOH833

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Functional Information from PROSITE/UniProt

site_id	PS00595
Number of Residues	21
Details	AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDAMytGSQKvlgappGiTpV

Chain	Residue	Details
A	ILE197-VAL217

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUF, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU

Chain	Residue	Details
A	SER78
B	SER78

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUU

Chain	Residue	Details
A	SER155
B	SER155

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU

Chain	Residue	Details
A	GLN205
B	GLN205

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU

Chain	Residue	Details
A	TYR257
A	THR260
B	TYR257
B	THR260

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI

Chain	Residue	Details
A	ARG356
B	ARG356

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|PIRSR:PIRSR000524-50, ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU

Chain	Residue	Details
A	LLP206
B	LLP206

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
A	LEU51

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
B	LEU51

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
A	ASP180
A	TRP105

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
B	ASP180
B	TRP105

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site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
A	HIS104
A	ASP180

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site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1bjo

Chain	Residue	Details
B	HIS104
B	ASP180

---