1P1R

Horse liver alcohol dehydrogenase complexed with NADH and R-N-1-methylhexylformamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
A	0004024	molecular_function	alcohol dehydrogenase (NAD+) activity, zinc-dependent
A	0004745	molecular_function	all-trans-retinol dehydrogenase (NAD+) activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0042572	biological_process	retinol metabolic process
A	0042573	biological_process	retinoic acid metabolic process
A	0046872	molecular_function	metal ion binding
B	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
B	0004024	molecular_function	alcohol dehydrogenase (NAD+) activity, zinc-dependent
B	0004745	molecular_function	all-trans-retinol dehydrogenase (NAD+) activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008270	molecular_function	zinc ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0042572	biological_process	retinol metabolic process
B	0042573	biological_process	retinoic acid metabolic process
B	0046872	molecular_function	metal ion binding
C	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
C	0004024	molecular_function	alcohol dehydrogenase (NAD+) activity, zinc-dependent
C	0004745	molecular_function	all-trans-retinol dehydrogenase (NAD+) activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008270	molecular_function	zinc ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0042572	biological_process	retinol metabolic process
C	0042573	biological_process	retinoic acid metabolic process
C	0046872	molecular_function	metal ion binding
D	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
D	0004024	molecular_function	alcohol dehydrogenase (NAD+) activity, zinc-dependent
D	0004745	molecular_function	all-trans-retinol dehydrogenase (NAD+) activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008270	molecular_function	zinc ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0042572	biological_process	retinol metabolic process
D	0042573	biological_process	retinoic acid metabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 375

Chain	Residue
A	CYS46
A	HIS67
A	CYS174
A	NAI377
A	NMH378

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 376

Chain	Residue
A	CYS97
A	CYS100
A	CYS103
A	CYS111

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 375

Chain	Residue
B	CYS46
B	HIS67
B	CYS174
B	NAI377
B	NMH378

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 376

Chain	Residue
B	CYS97
B	CYS100
B	CYS103
B	CYS111

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 375

Chain	Residue
C	CYS46
C	HIS67
C	CYS174
C	NAI377
C	NMH378

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 376

Chain	Residue
C	CYS97
C	CYS100
C	CYS103
C	CYS111

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 375

Chain	Residue
D	CYS46
D	HIS67
D	CYS174
D	NAI377
D	NMH378

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 376

Chain	Residue
D	CYS97
D	CYS100
D	CYS103
D	CYS111

---

site_id	AC9
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAI A 377

Chain	Residue
A	ARG47
A	SER48
A	HIS51
A	CYS174
A	THR178
A	GLY199
A	GLY201
A	GLY202
A	VAL203
A	ASP223
A	ILE224
A	VAL268
A	ILE269
A	ARG271
A	VAL292
A	GLY293
A	VAL294
A	ALA317
A	ILE318
A	PHE319
A	ARG369
A	ZN375
A	NMH378
A	HOH7025
A	HOH7045
A	HOH7046
A	HOH7155
A	HOH7218
A	HOH8024

---

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE NMH A 378

Chain	Residue
A	CYS46
A	SER48
A	LEU57
A	HIS67
A	PHE93
A	LEU116
A	CYS174
A	VAL294
A	ILE318
A	ZN375
A	NAI377
B	LEU309

---

site_id	BC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAI B 377

Chain	Residue
B	NMH378
B	HOH7727
B	HOH7747
B	HOH7748
B	HOH7875
B	HOH7891
B	HOH7915
B	HOH7923
B	ARG47
B	SER48
B	HIS51
B	CYS174
B	THR178
B	GLY199
B	GLY201
B	GLY202
B	VAL203
B	ASP223
B	ILE224
B	VAL268
B	ILE269
B	ARG271
B	VAL292
B	GLY293
B	VAL294
B	ALA317
B	ILE318
B	PHE319
B	ARG369
B	ZN375

---

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NMH B 378

Chain	Residue
A	LEU309
B	CYS46
B	SER48
B	HIS67
B	PHE93
B	LEU116
B	CYS174
B	VAL294
B	ILE318
B	ZN375
B	NAI377

---

site_id	BC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAI C 377

Chain	Residue
C	ARG47
C	SER48
C	HIS51
C	CYS174
C	THR178
C	GLY199
C	GLY201
C	GLY202
C	VAL203
C	ASP223
C	ILE224
C	VAL268
C	ILE269
C	ARG271
C	VAL292
C	GLY293
C	VAL294
C	ALA317
C	ILE318
C	PHE319
C	ARG369
C	ZN375
C	NMH378
C	HOH7256
C	HOH7260
C	HOH7277
C	HOH7278
C	HOH7391
C	HOH7462
C	HOH8104

---

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NMH C 378

Chain	Residue
C	CYS46
C	SER48
C	HIS67
C	PHE93
C	LEU116
C	CYS174
C	VAL294
C	ILE318
C	ZN375
C	NAI377
D	LEU309

---

site_id	BC6
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAI D 377

Chain	Residue
D	ARG47
D	SER48
D	HIS51
D	CYS174
D	THR178
D	GLY199
D	GLY201
D	GLY202
D	VAL203
D	ASP223
D	ILE224
D	LYS228
D	VAL268
D	ILE269
D	ARG271
D	VAL292
D	GLY293
D	VAL294
D	ALA317
D	ILE318
D	PHE319
D	ARG369
D	ZN375
D	NMH378
D	HOH7501
D	HOH7521
D	HOH7522
D	HOH7645
D	HOH7660
D	HOH7664
D	HOH7683
D	HOH7687

---

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NMH D 378

Chain	Residue
C	MET306
C	LEU309
D	CYS46
D	SER48
D	HIS67
D	PHE93
D	LEU116
D	CYS174
D	VAL294
D	ZN375
D	NAI377

---

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 2001

Chain	Residue
B	ARG218
B	GLU239
C	ARG218
C	THR238
C	GLU239

---

Functional Information from PROSITE/UniProt

site_id	PS00059
Number of Residues	15
Details	ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaAGIvesiGegV

Chain	Residue	Details
A	GLY66-VAL80

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0000269|PubMed:178875, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF, ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH, ECO:0007744|PDB:7ADH, ECO:0007744|PDB:8ADH

Chain	Residue	Details
A	ARG47
A	GLU68
B	ARG47
B	GLU68
C	ARG47
C	GLU68
D	ARG47
D	GLU68

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P06525

Chain	Residue	Details
A	ASP49
D	ASP49
D	GLY293
D	GLY320
A	GLY293
A	GLY320
B	ASP49
B	GLY293
B	GLY320
C	ASP49
C	GLY293
C	GLY320

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0000269|PubMed:178875, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF, ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH, ECO:0007744|PDB:7ADH, ECO:0007744|PDB:8ADH

Chain	Residue	Details
A	GLY98
C	ARG101
C	LYS104
C	LEU112
D	GLY98
D	ARG101
D	LYS104
D	LEU112
A	ARG101
A	LYS104
A	LEU112
B	GLY98
B	ARG101
B	LYS104
B	LEU112
C	GLY98

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1A72, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1ADC, ECO:0007744|PDB:1ADF, ECO:0007744|PDB:1ADG, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QLJ, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:1YE3, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH, ECO:0007744|PDB:7ADH, ECO:0007744|PDB:8ADH

Chain	Residue	Details
A	GLY175
B	GLY175
C	GLY175
D	GLY175

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:6ADH

Chain	Residue	Details
A	LEU200
B	LEU200
C	LEU200
D	LEU200

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QLH, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH

Chain	Residue	Details
A	ILE224
B	ILE224
C	ILE224
D	ILE224

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1QLH, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH

Chain	Residue	Details
A	PHE229
B	PHE229
C	PHE229
D	PHE229

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:6ADH

Chain	Residue	Details
A	THR370
B	THR370
C	THR370
D	THR370

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:5466062

Chain	Residue	Details
A	THR2
B	THR2
C	THR2
D	THR2

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	LEU57

---

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

Chain	Residue	Details
B	LEU57

---

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

Chain	Residue	Details
C	LEU57

---

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

Chain	Residue	Details
D	LEU57

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
A	SER48
A	HIS51

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
B	SER48
B	HIS51

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
C	SER48
C	HIS51

---

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
D	SER48
D	HIS51

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 256

Chain	Residue	Details
A	ARG47	metal ligand
A	ASP49	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	VAL52	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	GLU68	metal ligand
A	GLY175	metal ligand

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 256

Chain	Residue	Details
B	ARG47	metal ligand
B	ASP49	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	VAL52	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	GLU68	metal ligand
B	GLY175	metal ligand

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 256

Chain	Residue	Details
C	ARG47	metal ligand
C	ASP49	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	VAL52	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	GLU68	metal ligand
C	GLY175	metal ligand

---

site_id	MCSA4
Number of Residues	5
Details	M-CSA 256

Chain	Residue	Details
D	ARG47	metal ligand
D	ASP49	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	VAL52	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	GLU68	metal ligand
D	GLY175	metal ligand

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