Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ORD

Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from Thermotoga maritima at 1.40 A resolution

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	0008652	biological_process	amino acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
B	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
B	0005737	cellular_component	cytoplasm
B	0006525	biological_process	arginine metabolic process
B	0006526	biological_process	L-arginine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP A 401

Chain	Residue
A	GLY94
A	HOH438
A	HOH441
A	HOH446
A	HOH458
A	HOH480
A	HOH732
B	THR268
A	THR95
A	PHE126
A	HIS127
A	GLU178
A	ASP211
A	GLN214
A	LYS240
A	HOH432

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 401

Chain	Residue
A	THR268
A	HOH431
B	GLY94
B	THR95
B	ASN98
B	PHE126
B	HIS127
B	GLU178
B	ASP211
B	VAL213
B	GLN214
B	LYS240
B	HOH444
B	HOH452
B	HOH453
B	HOH469
B	HOH471

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 402

Chain	Residue
A	PHE291
A	LYS298
A	LEU364
A	THR365
A	GOL410
A	HOH467
A	HOH619
B	HOH588

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 403

Chain	Residue
A	ASN258
A	LEU260
A	HOH502
A	HOH579
A	HOH697

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 404

Chain	Residue
A	HIS-5
A	HIS-4
A	ALA12
A	THR13
A	ASP24
A	GLU25
A	HOH607
A	HOH612

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 405

Chain	Residue
A	TYR16
A	TYR23
A	HOH493
A	HOH660
B	GLU376

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 406

Chain	Residue
A	SER8
A	ARG337
A	THR341
A	HOH722
A	HOH744

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 407

Chain	Residue
A	TRP21
A	ASN346
A	LYS347
A	THR377
A	GOL408
A	HOH680
A	HOH710
B	GOL406

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 408

Chain	Residue
A	GOL407
A	HOH710
B	LYS347
B	HOH577
B	HOH668

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 409

Chain	Residue
A	GLU312
A	TYR313
A	HOH553
A	HOH724

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 410

Chain	Residue
A	GLU289
A	PHE291
A	GOL402
A	HOH765
B	GLU289
B	GOL402
B	HOH468

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 411

Chain	Residue
A	LYS110
A	GLU114
A	TYR117
A	HOH750
B	GLU147

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 412

Chain	Residue
A	LYS228
A	HOH716

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 402

Chain	Residue
B	LEU364
B	THR365
B	HOH450
A	GOL410
A	HOH619
B	PHE291
B	LYS298

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 403

Chain	Residue
A	TRP68
B	HIS0
B	LEU3
B	ASN5
B	HOH474
B	HOH524

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 404

Chain	Residue
B	SER8
B	PHE10
B	ARG337
B	HOH580
B	HOH615

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 405

Chain	Residue
A	GLU376
B	TYR16
B	TYR23
B	GLY27
B	HOH528
B	HOH689

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 406

Chain	Residue
A	GLU376
A	THR377
A	GOL407
A	HOH707
B	GLY27
B	HOH508
B	HOH689

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 407

Chain	Residue
A	MSE1
A	TYR2
B	SER80
B	GLY85
B	GLY86
B	LYS87
B	HOH522
B	HOH703

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	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase from Thermotoga maritima.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11) (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase from Thermotoga maritima.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11) (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11) (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	PHE126
B	ASP211

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	PHE126
A	ASP211
A	LYS240

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	PHE126
B	ASP211
B	LYS240

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	ARG48

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	ARG48

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)