1H0C

The crystal structure of human alanine:glyoxylate aminotransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004760	molecular_function	serine-pyruvate transaminase activity
A	0005515	molecular_function	protein binding
A	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0005829	cellular_component	cytosol
A	0006563	biological_process	L-serine metabolic process
A	0007219	biological_process	Notch signaling pathway
A	0008453	molecular_function	alanine-glyoxylate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0009436	biological_process	glyoxylate catabolic process
A	0016597	molecular_function	amino acid binding
A	0016740	molecular_function	transferase activity
A	0019265	biological_process	glycine biosynthetic process, by transamination of glyoxylate
A	0019448	biological_process	L-cysteine catabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0042853	biological_process	L-alanine catabolic process
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0043621	molecular_function	obsolete protein self-association
A	0046487	biological_process	glyoxylate metabolic process
A	0046724	biological_process	oxalic acid secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 1391

Chain	Residue
A	SER81
A	GLN208
A	LYS209
A	TYR260
A	THR263
A	AOA1392
A	GLY82
A	HIS83
A	TRP108
A	GLY156
A	SER158
A	ASP183
A	VAL185
A	ALA186

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AOA A 1392

Chain	Residue
A	PRO28
A	GLY29
A	SER158
A	LYS209
A	LEU351
A	ARG360
A	PLP1391
A	HOH2098
A	HOH2141

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1393

Chain	Residue
A	ARG333
A	VAL336
A	SER337

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1394

Chain	Residue
A	LEU7
A	LEU24
A	ARG71
A	ASP196
A	PHE343
A	HOH2137

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1395

Chain	Residue
A	LYS228
A	GLN290
A	GLU293
A	THR369
A	ARG370
A	GLU371

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1396

Chain	Residue
A	PRO17
A	SER19
A	ASP52
A	GLN55

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1397

Chain	Residue
A	ILE107
A	GLN110
A	ARG111
A	ASP114

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 1398

Chain	Residue
A	HOH2020
A	HOH2143

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE200-ILE220

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	ARG360

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR9

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine

Chain	Residue	Details
A	LYS209

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:O35423

Chain	Residue	Details
A	LYS225

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O35423

Chain	Residue	Details
A	LYS234
A	LYS312

---