Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4B9B

The structure of the omega aminotransferase from Pseudomonas aeruginosa

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0009102	biological_process	biotin biosynthetic process
A	0016223	molecular_function	beta-alanine-pyruvate transaminase activity
A	0019483	biological_process	beta-alanine biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
B	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009102	biological_process	biotin biosynthetic process
B	0016223	molecular_function	beta-alanine-pyruvate transaminase activity
B	0019483	biological_process	beta-alanine biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
C	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009102	biological_process	biotin biosynthetic process
C	0016223	molecular_function	beta-alanine-pyruvate transaminase activity
C	0019483	biological_process	beta-alanine biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
D	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009102	biological_process	biotin biosynthetic process
D	0016223	molecular_function	beta-alanine-pyruvate transaminase activity
D	0019483	biological_process	beta-alanine biosynthetic process
D	0030170	molecular_function	pyridoxal phosphate binding
E	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
E	0008483	molecular_function	transaminase activity
E	0009102	biological_process	biotin biosynthetic process
E	0016223	molecular_function	beta-alanine-pyruvate transaminase activity
E	0019483	biological_process	beta-alanine biosynthetic process
E	0030170	molecular_function	pyridoxal phosphate binding
F	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
F	0008483	molecular_function	transaminase activity
F	0009102	biological_process	biotin biosynthetic process
F	0016223	molecular_function	beta-alanine-pyruvate transaminase activity
F	0019483	biological_process	beta-alanine biosynthetic process
F	0030170	molecular_function	pyridoxal phosphate binding
G	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
G	0008483	molecular_function	transaminase activity
G	0009102	biological_process	biotin biosynthetic process
G	0016223	molecular_function	beta-alanine-pyruvate transaminase activity
G	0019483	biological_process	beta-alanine biosynthetic process
G	0030170	molecular_function	pyridoxal phosphate binding
H	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
H	0008483	molecular_function	transaminase activity
H	0009102	biological_process	biotin biosynthetic process
H	0016223	molecular_function	beta-alanine-pyruvate transaminase activity
H	0019483	biological_process	beta-alanine biosynthetic process
H	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE PLP A 500

Chain	Residue
A	SER119
A	ILE262
A	LYS288
A	HOH2098
A	HOH2218
A	HOH2221
A	HOH2300
A	HOH2422
A	HOH2462
A	HOH2487
A	HOH2647
A	GLY120
A	HOH2648
B	TYR326
B	THR327
A	SER121
A	TYR153
A	HIS154
A	GLY155
A	GLU226
A	ASP259
A	VAL261

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 501

Chain	Residue
A	THR193
A	ALA197
A	GLN198
A	THR199
A	HOH2649
A	HOH2650

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 502

Chain	Residue
A	SER323
A	HOH2509
A	HOH2511
B	MET172
B	PHE173

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 504

Chain	Residue
A	ALA150
A	HIS181
A	PRO183
A	HOH2347
A	HOH2351
A	HOH2652
A	HOH2653
A	HOH2654
G	LYS210
G	LEU211

site_id	AC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE PLP B 500

Chain	Residue
A	TYR326
A	THR327
A	HOH2513
A	HOH2514
A	HOH2515
A	HOH2517
B	SER119
B	GLY120
B	SER121
B	TYR153
B	HIS154
B	GLY155
B	GLU226
B	ASP259
B	VAL261
B	ILE262
B	LYS288
B	HOH2164
B	HOH2166
B	HOH2228
B	HOH2343
B	HOH2398

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL B 502

Chain	Residue
A	MET172
A	PHE173
B	SER323
B	HOH2418
B	HOH2419

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL B 504

Chain	Residue
B	ALA150
B	HIS181
B	PRO183
B	HOH2275
B	HOH2279
B	HOH2534
B	HOH2535
B	HOH2536
H	LYS210
H	LEU211
H	LEU214

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PLP C 500

Chain	Residue
D	TYR326
D	THR327
C	SER119
C	GLY120
C	SER121
C	TYR153
C	HIS154
C	GLY155
C	GLU226
C	ASP259
C	VAL261
C	ILE262
C	LYS288
C	HOH2245
C	HOH2246
C	HOH2250
C	HOH2476
C	HOH2537
C	HOH2709
C	HOH2710

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 501

Chain	Residue
C	MET190
C	THR193
C	GLN198
C	THR199
C	HOH2711
C	HOH2713

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 502

Chain	Residue
C	SER323
C	HOH2560
C	HOH2563
D	MET172
D	PHE173

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL C 504

Chain	Residue
C	LYS210
C	LEU211
C	HOH2399
C	HOH2400
C	HOH2453
C	HOH2456
C	HOH2715
C	HOH2718
E	ALA150
E	HIS181
E	GOL504

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PLP D 500

Chain	Residue
C	TYR326
C	THR327
C	HOH2564
C	HOH2565
C	HOH2566
C	HOH2568
D	SER119
D	GLY120
D	SER121
D	TYR153
D	HIS154
D	GLY155
D	GLU226
D	ASP259
D	VAL261
D	ILE262
D	LYS288
D	HOH2183
D	HOH2184
D	HOH2377
D	HOH2438

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D 502

Chain	Residue
C	MET172
C	PHE173
D	SER323
D	HOH2458
D	HOH2460

site_id	BC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE PLP E 500

Chain	Residue
E	SER119
E	GLY120
E	SER121
E	TYR153
E	HIS154
E	GLY155
E	GLU226
E	ASP259
E	VAL261
E	ILE262
E	LYS288
E	HOH2217
E	HOH2219
E	HOH2222
E	HOH2290
E	HOH2385
E	HOH2450
E	HOH2605
E	HOH2606
E	HOH2607
F	TYR326
F	THR327

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL E 502

Chain	Residue
E	SER323
E	HOH2474
E	HOH2476
F	MET172
F	PHE173

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 503

Chain	Residue
C	ASP180
C	HOH2398
C	HOH2399
C	HOH2400
C	HOH2717
E	ASP180

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL E 504

Chain	Residue
C	ALA150
C	HIS181
C	GOL504
C	HOH2398
C	HOH2717
C	HOH2718
E	LEU211
E	HOH2367
E	HOH2372
E	HOH2608

site_id	BC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PLP F 500

Chain	Residue
E	TYR326
E	THR327
E	HOH2478
E	HOH2479
E	HOH2480
F	SER119
F	GLY120
F	SER121
F	TYR153
F	HIS154
F	GLY155
F	GLU226
F	ASP259
F	VAL261
F	ILE262
F	LYS288
F	HOH2158
F	HOH2159
F	HOH2225
F	HOH2310
F	HOH2371

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 501

Chain	Residue
F	MET190
F	THR193
F	ALA197
F	GLN198
F	THR199
F	HOH2515

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL F 502

Chain	Residue
E	MET172
E	PHE173
F	SER323
F	HOH2388
F	HOH2389

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 503

Chain	Residue
D	ASP180
D	HOH2298
D	HOH2299
D	HOH2300
F	ASP180
F	HOH2251

site_id	CC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE PLP G 500

Chain	Residue
G	SER119
G	GLY120
G	SER121
G	TYR153
G	HIS154
G	GLY155
G	GLU226
G	ASP259
G	VAL261
G	ILE262
G	LYS288
G	HOH2172
G	HOH2173
G	HOH2176
G	HOH2237
G	HOH2239
G	HOH2325
G	HOH2383
G	HOH2530
G	HOH2531
H	TYR326
H	THR327

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL G 502

Chain	Residue
G	SER323
G	HOH2404
G	HOH2407
H	MET172
H	PHE173

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA G 503

Chain	Residue
A	ASP180
A	HOH2346
A	HOH2347
A	HOH2348
G	ASP180
G	HOH2265

site_id	CC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL G 504

Chain	Residue
A	LYS210
A	LEU211
A	HOH2346
A	HOH2400
A	HOH2403
G	HIS181
G	PRO183
G	HOH2267
G	HOH2532

site_id	CC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE PLP H 500

Chain	Residue
G	TYR326
G	THR327
G	HOH2409
G	HOH2410
G	HOH2411
G	HOH2413
H	SER119
H	GLY120
H	SER121
H	TYR153
H	HIS154
H	GLY155
H	GLU226
H	ASP259
H	VAL261
H	ILE262
H	LYS288
H	HOH2141
H	HOH2143
H	HOH2189
H	HOH2266
H	HOH2321

site_id	CC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL H 501

Chain	Residue
H	THR193
H	ALA197
H	GLN198
H	THR199
H	HOH2436
H	HOH2437

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL H 502

Chain	Residue
G	MET172
G	PHE173
H	SER323
H	HOH2340
H	HOH2342

site_id	DC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA H 503

Chain	Residue
B	ASP180
B	HOH2274
B	HOH2275
B	HOH2276
H	ASP180
H	HOH2209

site_id	DC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL H 504

Chain	Residue
B	LYS210
B	HOH2276
B	HOH2318
B	HOH2324
H	HIS181
H	PRO183
H	HOH2209
H	HOH2211
H	HOH2439

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVit.AFgRlGtysgaeyfgvtp....DLMnvAKqvtNG

Chain	Residue	Details
A	LEU256-GLY293

site_id	PS00639
Number of Residues	11
Details	THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GYHGVNVAGTS

Chain	Residue	Details
A	GLY152-SER162

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:23519665

Chain	Residue	Details
A	TRP61
D	TRP61
D	ARG414
D	GLN421
E	TRP61
E	ARG414
E	GLN421
F	TRP61
F	ARG414
F	GLN421
G	TRP61
A	ARG414
G	ARG414
G	GLN421
H	TRP61
H	ARG414
H	GLN421
A	GLN421
B	TRP61
B	ARG414
B	GLN421
C	TRP61
C	ARG414
C	GLN421

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	GLY120
B	GLY120
C	GLY120
D	GLY120
E	GLY120
F	GLY120
G	GLY120
H	GLY120

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:23519665, ECO:0000269\|Ref.4

Chain	Residue	Details
A	THR327
B	THR327
C	THR327
D	THR327
E	THR327
F	THR327
G	THR327
H	THR327

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N6-(pyridoxal phosphate)lysine

Chain	Residue	Details
A	LYS288
B	LYS288
C	LYS288
D	LYS288
E	LYS288
F	LYS288
G	LYS288
H	LYS288

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