Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1H5Q

Mannitol dehydrogenase from Agaricus bisporus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0019594	biological_process	mannitol metabolic process
A	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
A	0050661	molecular_function	NADP binding
A	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
A	0051289	biological_process	protein homotetramerization
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0019594	biological_process	mannitol metabolic process
B	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
B	0050661	molecular_function	NADP binding
B	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
B	0051289	biological_process	protein homotetramerization
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0019594	biological_process	mannitol metabolic process
C	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
C	0050661	molecular_function	NADP binding
C	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
C	0051289	biological_process	protein homotetramerization
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0019594	biological_process	mannitol metabolic process
D	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
D	0050661	molecular_function	NADP binding
D	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
D	0051289	biological_process	protein homotetramerization
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0019594	biological_process	mannitol metabolic process
E	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
E	0050661	molecular_function	NADP binding
E	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
E	0051289	biological_process	protein homotetramerization
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0019594	biological_process	mannitol metabolic process
F	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
F	0050661	molecular_function	NADP binding
F	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
F	0051289	biological_process	protein homotetramerization
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0019594	biological_process	mannitol metabolic process
G	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
G	0050661	molecular_function	NADP binding
G	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
G	0051289	biological_process	protein homotetramerization
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0019594	biological_process	mannitol metabolic process
H	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
H	0050661	molecular_function	NADP binding
H	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
H	0051289	biological_process	protein homotetramerization
I	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
I	0019594	biological_process	mannitol metabolic process
I	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
I	0050661	molecular_function	NADP binding
I	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
I	0051289	biological_process	protein homotetramerization
J	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
J	0019594	biological_process	mannitol metabolic process
J	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
J	0050661	molecular_function	NADP binding
J	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
J	0051289	biological_process	protein homotetramerization
K	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
K	0019594	biological_process	mannitol metabolic process
K	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
K	0050661	molecular_function	NADP binding
K	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
K	0051289	biological_process	protein homotetramerization
L	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
L	0019594	biological_process	mannitol metabolic process
L	0050085	molecular_function	mannitol 2-dehydrogenase (NADP+) activity
L	0050661	molecular_function	NADP binding
L	0050664	molecular_function	oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
L	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI A2263

Chain	Residue
A	TRP262
A	HOH2125
A	HOH2127
C	TRP262
C	HOH2241
C	HOH2243

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI B2263

Chain	Residue
D	TRP262
D	HOH2183
D	HOH2184
B	TRP262
B	HOH2193
B	HOH2195

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI E3263

Chain	Residue
E	TRP262
E	HOH2329
E	HOH2333
G	TRP262
G	HOH2278
G	HOH2281

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI F3263

Chain	Residue
F	TRP262
F	HOH2304
F	HOH2306
H	TRP262
H	HOH2290
H	HOH2291

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI I3263

Chain	Residue
I	TRP262
I	HOH2299
I	HOH2300
K	TRP262
K	HOH2273
K	HOH2275

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI J3263

Chain	Residue
J	TRP262
J	HOH2257
J	HOH2260
L	TRP262
L	HOH2295
L	HOH2297

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP A 263

Chain	Residue
A	ASN20
A	ARG21
A	GLY22
A	ILE23
A	TYR42
A	ARG43
A	SER44
A	ALA45
A	CYS68
A	ASP69
A	VAL70
A	ASN96
A	ALA97
A	GLY98
A	VAL99
A	VAL119
A	SER148
A	SER149
A	TYR169
A	LYS173
A	GLY200
A	VAL202
A	GLN206
A	HOH2128
A	HOH2129
A	HOH2130

site_id	AC8
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAP B 263

Chain	Residue
B	GLY18
B	ASN20
B	ARG21
B	GLY22
B	ILE23
B	TYR42
B	ARG43
B	SER44
B	ALA45
B	CYS68
B	ASP69
B	VAL70
B	ASN96
B	ALA97
B	GLY98
B	THR147
B	SER148
B	SER149
B	TYR169
B	LYS173
B	PRO199
B	GLY200
B	VAL202
B	THR204
B	GLN206
B	THR207
B	HOH2030
B	HOH2033
B	HOH2087
B	HOH2197
B	HOH2198
B	HOH2199
B	HOH2200
B	HOH2201

site_id	AC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAP C 263

Chain	Residue
C	ILE23
C	TYR42
C	ARG43
C	SER44
C	ALA45
C	CYS68
C	ASP69
C	VAL70
C	ASN96
C	ALA97
C	GLY98
C	THR147
C	SER148
C	TYR169
C	LYS173
C	PRO199
C	GLY200
C	VAL202
C	GLN206
C	HOH2047
C	HOH2114
C	HOH2197
C	HOH2246
C	HOH2247
C	HOH2248
C	HOH2249
C	HOH2250
C	ASN20
C	ARG21
C	GLY22

site_id	BC1
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAP D 263

Chain	Residue
D	GLY18
D	ASN20
D	ARG21
D	GLY22
D	ILE23
D	TYR42
D	ARG43
D	SER44
D	ALA45
D	CYS68
D	ASP69
D	VAL70
D	ASN96
D	ALA97
D	GLY98
D	VAL99
D	VAL119
D	THR147
D	SER148
D	SER149
D	TYR169
D	LYS173
D	PRO199
D	GLY200
D	VAL202
D	GLN206
D	HOH2026
D	HOH2140
D	HOH2144
D	HOH2186
D	HOH2187
D	HOH2188
D	HOH2189
D	HOH2190

site_id	BC2
Number of Residues	36
Details	BINDING SITE FOR RESIDUE NAP E 263

Chain	Residue
E	GLY18
E	ASN20
E	ARG21
E	GLY22
E	ILE23
E	TYR42
E	ARG43
E	SER44
E	ALA45
E	CYS68
E	ASP69
E	VAL70
E	ASN96
E	ALA97
E	GLY98
E	VAL119
E	THR147
E	SER148
E	SER149
E	TYR169
E	LYS173
E	PRO199
E	GLY200
E	VAL202
E	GLN206
E	HOH2072
E	HOH2077
E	HOH2271
E	HOH2334
E	HOH2335
E	HOH2336
E	HOH2337
E	HOH2338
E	HOH2339
E	HOH2341
E	HOH2342

site_id	BC3
Number of Residues	36
Details	BINDING SITE FOR RESIDUE NAP F 263

Chain	Residue
F	GLY18
F	ASN20
F	ARG21
F	GLY22
F	ILE23
F	TYR42
F	ARG43
F	SER44
F	ALA45
F	CYS68
F	ASP69
F	VAL70
F	ASN96
F	ALA97
F	GLY98
F	VAL119
F	THR147
F	SER148
F	SER149
F	TYR169
F	LYS173
F	PRO199
F	GLY200
F	VAL202
F	GLN206
F	HOH2059
F	HOH2062
F	HOH2151
F	HOH2236
F	HOH2240
F	HOH2307
F	HOH2308
F	HOH2309
F	HOH2310
F	HOH2312
F	HOH2313

site_id	BC4
Number of Residues	37
Details	BINDING SITE FOR RESIDUE NAP G 263

Chain	Residue
G	GLY18
G	ASN20
G	ARG21
G	GLY22
G	ILE23
G	ARG43
G	SER44
G	ALA45
G	CYS68
G	ASP69
G	VAL70
G	ASN96
G	ALA97
G	GLY98
G	VAL119
G	THR147
G	SER148
G	SER149
G	TYR169
G	LYS173
G	PRO199
G	GLY200
G	VAL202
G	GLN206
G	HOH2030
G	HOH2058
G	HOH2059
G	HOH2067
G	HOH2227
G	HOH2282
G	HOH2283
G	HOH2284
G	HOH2286
G	HOH2287
G	HOH2289
G	HOH2290
G	HOH2291

site_id	BC5
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAP H 263

Chain	Residue
H	ASN20
H	ARG21
H	GLY22
H	ILE23
H	TYR42
H	ARG43
H	SER44
H	ALA45
H	CYS68
H	ASP69
H	VAL70
H	ASN96
H	ALA97
H	GLY98
H	VAL119
H	THR147
H	SER148
H	SER149
H	TYR169
H	LYS173
H	PRO199
H	GLY200
H	VAL202
H	GLN206
H	HOH2054
H	HOH2059
H	HOH2232
H	HOH2293
H	HOH2294
H	HOH2295
H	HOH2296
H	HOH2297
H	HOH2298
H	HOH2300
H	HOH2302

site_id	BC6
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAP I 263

Chain	Residue
I	ASN20
I	ARG21
I	GLY22
I	ILE23
I	TYR42
I	ARG43
I	SER44
I	ALA45
I	CYS68
I	ASP69
I	VAL70
I	ASN96
I	ALA97
I	GLY98
I	VAL119
I	THR147
I	SER148
I	SER149
I	TYR169
I	LYS173
I	PRO199
I	GLY200
I	VAL202
I	GLN206
I	HOH2062
I	HOH2063
I	HOH2241
I	HOH2302
I	HOH2303
I	HOH2304
I	HOH2305
I	HOH2306
I	HOH2307
I	HOH2308

site_id	BC7
Number of Residues	37
Details	BINDING SITE FOR RESIDUE NAP J 263

Chain	Residue
J	GLY18
J	ASN20
J	ARG21
J	GLY22
J	ILE23
J	TYR42
J	ARG43
J	SER44
J	ALA45
J	CYS68
J	ASP69
J	VAL70
J	ASN96
J	ALA97
J	GLY98
J	VAL119
J	THR147
J	SER148
J	SER149
J	TYR169
J	LYS173
J	PRO199
J	GLY200
J	VAL202
J	GLN206
J	HOH2023
J	HOH2044
J	HOH2163
J	HOH2205
J	HOH2261
J	HOH2262
J	HOH2263
J	HOH2264
J	HOH2265
J	HOH2266
J	HOH2267
J	HOH2268

site_id	BC8
Number of Residues	38
Details	BINDING SITE FOR RESIDUE NAP K 263

Chain	Residue
K	GLY18
K	ASN20
K	ARG21
K	GLY22
K	ILE23
K	TYR42
K	ARG43
K	SER44
K	ALA45
K	CYS68
K	ASP69
K	VAL70
K	ASN96
K	ALA97
K	GLY98
K	VAL119
K	THR147
K	SER148
K	SER149
K	TYR169
K	LYS173
K	PRO199
K	GLY200
K	VAL202
K	THR204
K	GLN206
K	HOH2046
K	HOH2049
K	HOH2136
K	HOH2221
K	HOH2276
K	HOH2277
K	HOH2278
K	HOH2279
K	HOH2281
K	HOH2282
K	HOH2283
K	HOH2284

site_id	BC9
Number of Residues	36
Details	BINDING SITE FOR RESIDUE NAP L 263

Chain	Residue
L	ASN20
L	ARG21
L	GLY22
L	ILE23
L	TYR42
L	ARG43
L	SER44
L	ALA45
L	CYS68
L	ASP69
L	VAL70
L	ASN96
L	ALA97
L	GLY98
L	VAL99
L	THR147
L	SER148
L	SER149
L	TYR169
L	LYS173
L	PRO199
L	GLY200
L	VAL202
L	GLN206
L	HOH2060
L	HOH2061
L	HOH2235
L	HOH2239
L	HOH2299
L	HOH2300
L	HOH2301
L	HOH2302
L	HOH2303
L	HOH2304
L	HOH2305
L	HOH2306

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11335726","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11335726","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Active site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"PubMed","id":"11335726","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"L0E2Z4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11335726","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H5Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	SER149
A	TYR169
A	LYS173

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
J	SER149
J	TYR169
J	LYS173

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
K	SER149
K	TYR169
K	LYS173

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
L	SER149
L	TYR169
L	LYS173

site_id	CSA13
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	ASN120
A	TYR169
A	SER149
A	LYS173

site_id	CSA14
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	ASN120
B	TYR169
B	SER149
B	LYS173

site_id	CSA15
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	ASN120
C	TYR169
C	SER149
C	LYS173

site_id	CSA16
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	ASN120
D	TYR169
D	SER149
D	LYS173

site_id	CSA17
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
E	ASN120
E	TYR169
E	SER149
E	LYS173

site_id	CSA18
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
F	ASN120
F	TYR169
F	SER149
F	LYS173

site_id	CSA19
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
G	ASN120
G	TYR169
G	SER149
G	LYS173

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	SER149
B	TYR169
B	LYS173

site_id	CSA20
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
H	ASN120
H	TYR169
H	SER149
H	LYS173

site_id	CSA21
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
I	ASN120
I	TYR169
I	SER149
I	LYS173

site_id	CSA22
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
J	ASN120
J	TYR169
J	SER149
J	LYS173

site_id	CSA23
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
K	ASN120
K	TYR169
K	SER149
K	LYS173

site_id	CSA24
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
L	ASN120
L	TYR169
L	SER149
L	LYS173

site_id	CSA25
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	TYR169
A	LYS173

site_id	CSA26
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	TYR169
B	LYS173

site_id	CSA27
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	TYR169
C	LYS173

site_id	CSA28
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	TYR169
D	LYS173

site_id	CSA29
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
E	TYR169
E	LYS173

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	SER149
C	TYR169
C	LYS173

site_id	CSA30
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
F	TYR169
F	LYS173

site_id	CSA31
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
G	TYR169
G	LYS173

site_id	CSA32
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
H	TYR169
H	LYS173

site_id	CSA33
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
I	TYR169
I	LYS173

site_id	CSA34
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
J	TYR169
J	LYS173

site_id	CSA35
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
K	TYR169
K	LYS173

site_id	CSA36
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
L	TYR169
L	LYS173

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	SER149
D	TYR169
D	LYS173

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
E	SER149
E	TYR169
E	LYS173

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
F	SER149
F	TYR169
F	LYS173

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
G	SER149
G	TYR169
G	LYS173

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
H	SER149
H	TYR169
H	LYS173

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
I	SER149
I	TYR169
I	LYS173

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