Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1HF3

ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING Cadmium and a hydroxide adduct to NADH

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CD A 400

Chain	Residue
A	CYS46
A	HIS67
A	GLU68
A	CYS174
A	NAD402
A	HOH2024
A	HOH2025

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 401

Chain	Residue
A	CYS103
A	CYS111
A	CYS97
A	CYS100

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CD B 400

Chain	Residue
B	CYS46
B	HIS67
B	CYS174
B	NAD402
B	HOH2019
B	HOH2020

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 401

Chain	Residue
B	CYS97
B	CYS100
B	CYS103
B	CYS111

site_id	AC5
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD A 402

Chain	Residue
A	ARG47
A	SER48
A	HIS51
A	CYS174
A	THR178
A	GLY199
A	LEU200
A	GLY201
A	GLY202
A	VAL203
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	CD400
A	MRD403
A	HOH2025
A	HOH2069
A	HOH2116
A	HOH2117
A	HOH2118

site_id	AC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD B 402

Chain	Residue
B	ARG47
B	SER48
B	HIS51
B	CYS174
B	THR178
B	GLY199
B	GLY201
B	GLY202
B	VAL203
B	ASP223
B	ILE224
B	LYS228
B	VAL268
B	ILE269
B	ARG271
B	VAL292
B	GLY293
B	VAL294
B	ALA317
B	ILE318
B	PHE319
B	LEU362
B	ARG369
B	CD400
B	HOH2019
B	HOH2089
B	HOH2147
B	HOH2149
B	HOH2150
B	HOH2151

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MRD A 403

Chain	Residue
A	SER48
A	LEU57
A	LEU116
A	VAL294
A	NAD402
A	HOH2024

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MRD B 403

Chain	Residue
B	SER48
B	LEU57
B	LEU141
B	VAL294
B	HOH2020
B	HOH2152
B	HOH2153

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	4
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

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P06525

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

site_id	SWS_FT_FI3
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: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
A	ARG101
A	LYS104
A	LEU112
B	GLY98
B	ARG101
B	LYS104
B	LEU112

site_id	SWS_FT_FI4
Number of Residues	2
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

site_id	SWS_FT_FI5
Number of Residues	2
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

site_id	SWS_FT_FI6
Number of Residues	2
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

site_id	SWS_FT_FI7
Number of Residues	2
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

site_id	SWS_FT_FI8
Number of Residues	2
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

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000269\|PubMed:5466062

Chain	Residue	Details
A	THR2
B	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	2
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
A	SER48
A	HIS51

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1guf

Chain	Residue	Details
B	SER48
B	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

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