2E54

Crystal structure of acetylornithine aminotransferase from Thermotoga maritima

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
A	0005737	cellular_component	cytoplasm
A	0006525	biological_process	arginine metabolic process
A	0006526	biological_process	L-arginine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA A 1004

Chain	Residue
A	LYS310
A	TYR313
A	VAL316
A	NA1005
A	HOH1043
A	HOH1071
A	HOH1073

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA A 1005

Chain	Residue
A	HOH1071
A	HOH1073
A	HOH1203
A	HOH1392
A	HOH1474
A	NA1004
A	HOH1043

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PLP A 1001

Chain	Residue
A	THR93
A	GLY94
A	THR95
A	PHE126
A	HIS127
A	GLU178
A	GLU183
A	ASP211
A	VAL213
A	GLN214
A	LYS240
A	THR268
A	HOH1024
A	HOH1029
A	HOH1030
A	HOH1037
A	HOH1040
A	HOH1075

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1002

Chain	Residue
A	GLU294
A	LYS298
A	LEU364
A	THR365
A	HOH1173
A	HOH1336

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1003

Chain	Residue
A	ASP32
A	SER35
A	ASN40
A	HIS44
A	PRO363

---

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVqc.GMgRtGklfayqkygvvp....DVLttAKglgGG

Chain	Residue	Details
A	LEU208-GLY245

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|Ref.2, ECO:0000269|Ref.3

Chain	Residue	Details
A	GLY94

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305|Ref.2, ECO:0000305|Ref.3

Chain	Residue	Details
A	PHE126
A	ASP211

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107

Chain	Residue	Details
A	ARG129
A	THR267

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|Ref.3

Chain	Residue	Details
A	THR268

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01107

Chain	Residue	Details
A	LYS240

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	PHE126
A	ASP211

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	PHE126
A	ASP211
A	LYS240

---

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	ARG48

---