1AXG

CRYSTAL STRUCTURE OF THE VAL203->ALA MUTANT OF LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH COFACTOR NAD AND INHIBITOR TRIFLUOROETHANOL SOLVED TO 2.5 ANGSTROM RESOLUTION

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 401

Chain	Residue
A	CYS46
A	HIS67
A	CYS174
A	NAD403
A	ETF404

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 402

Chain	Residue
A	CYS97
A	CYS100
A	CYS103
A	CYS111

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 401

Chain	Residue
B	CYS46
B	SER48
B	HIS67
B	CYS174
B	NAD403
B	ETF404

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 402

Chain	Residue
B	CYS97
B	CYS100
B	CYS103
B	CYS111

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN C 401

Chain	Residue
C	CYS46
C	SER48
C	HIS67
C	CYS174
C	NAD403
C	ETF404

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 402

Chain	Residue
C	CYS97
C	CYS100
C	CYS103
C	CYS111

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN D 401

Chain	Residue
D	CYS46
D	SER48
D	HIS67
D	CYS174
D	NAD403
D	ETF404

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 402

Chain	Residue
D	CYS97
D	CYS100
D	CYS103
D	CYS111

---

site_id	AC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD A 403

Chain	Residue
A	ARG47
A	SER48
A	HIS51
A	CYS174
A	THR178
A	GLY199
A	GLY201
A	GLY202
A	ALA203
A	ASP223
A	ILE224
A	LYS228
A	VAL268
A	ILE269
A	ARG271
A	VAL292
A	GLY293
A	VAL294
A	ALA317
A	ILE318
A	PHE319
A	ARG369
A	ZN401
A	ETF404
A	HOH405
A	HOH476
A	HOH487

---

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ETF A 404

Chain	Residue
A	SER48
A	HIS67
A	PHE93
A	LEU116
A	LEU141
A	CYS174
A	VAL294
A	ZN401
A	NAD403

---

site_id	BC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD B 403

Chain	Residue
B	HOH406
B	HOH458
A	LEU309
B	ARG47
B	SER48
B	HIS51
B	CYS174
B	THR178
B	GLY199
B	GLY201
B	GLY202
B	ALA203
B	VAL222
B	ASP223
B	ILE224
B	LYS228
B	VAL268
B	ILE269
B	VAL292
B	GLY293
B	VAL294
B	ALA317
B	ILE318
B	PHE319
B	ARG369
B	ZN401

---

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ETF B 404

Chain	Residue
B	SER48
B	LEU57
B	HIS67
B	PHE93
B	LEU116
B	LEU141
B	VAL294
B	ZN401

---

site_id	BC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD C 403

Chain	Residue
C	ARG47
C	SER48
C	HIS51
C	CYS174
C	THR178
C	GLY199
C	GLY201
C	GLY202
C	ALA203
C	ASP223
C	ILE224
C	LYS228
C	VAL268
C	ILE269
C	ARG271
C	VAL292
C	GLY293
C	VAL294
C	ALA317
C	ILE318
C	PHE319
C	ARG369
C	ZN401
C	ETF404
C	HOH412
C	HOH474
C	HOH475

---

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ETF C 404

Chain	Residue
C	SER48
C	HIS67
C	PHE93
C	LEU116
C	LEU141
C	ZN401
C	NAD403

---

site_id	BC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD D 403

Chain	Residue
C	LEU309
D	ARG47
D	SER48
D	HIS51
D	CYS174
D	THR178
D	GLY199
D	GLY201
D	GLY202
D	ALA203
D	ASP223
D	ILE224
D	LYS228
D	VAL268
D	ILE269
D	GLY270
D	ARG271
D	VAL292
D	GLY293
D	VAL294
D	ALA317
D	ILE318
D	PHE319
D	LEU362
D	ARG369
D	ZN401
D	ETF404
D	HOH405
D	HOH474
D	HOH475

---

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ETF D 404

Chain	Residue
D	SER48
D	LEU57
D	HIS67
D	PHE93
D	LEU116
D	LEU141
D	CYS174
D	VAL294
D	ZN401
D	NAD403

---

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

---