Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3COS

Crystal structure of human class II alcohol dehydrogenase (ADH4) in complex with NAD and Zn

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
A	0003960	molecular_function	quinone reductase (NADPH) activity
A	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
A	0004032	molecular_function	aldose reductase (NADPH) activity
A	0004745	molecular_function	all-trans-retinol dehydrogenase (NAD+) activity
A	0005503	molecular_function	all-trans retinal binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006066	biological_process	alcohol metabolic process
A	0006081	biological_process	aldehyde metabolic process
A	0006629	biological_process	lipid metabolic process
A	0008270	molecular_function	zinc ion binding
A	0010430	biological_process	fatty acid omega-oxidation
A	0016491	molecular_function	oxidoreductase activity
A	0018479	molecular_function	benzaldehyde dehydrogenase (NAD+) activity
A	0019841	molecular_function	retinol binding
A	0042572	biological_process	retinol metabolic process
A	0046164	biological_process	alcohol catabolic process
A	0046294	biological_process	formaldehyde catabolic process
A	0046872	molecular_function	metal ion binding
A	0051287	molecular_function	NAD binding
A	0051903	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
A	1901661	biological_process	quinone metabolic process
B	0001523	biological_process	retinoid metabolic process
B	0003960	molecular_function	quinone reductase (NADPH) activity
B	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
B	0004032	molecular_function	aldose reductase (NADPH) activity
B	0004745	molecular_function	all-trans-retinol dehydrogenase (NAD+) activity
B	0005503	molecular_function	all-trans retinal binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006066	biological_process	alcohol metabolic process
B	0006081	biological_process	aldehyde metabolic process
B	0006629	biological_process	lipid metabolic process
B	0008270	molecular_function	zinc ion binding
B	0010430	biological_process	fatty acid omega-oxidation
B	0016491	molecular_function	oxidoreductase activity
B	0018479	molecular_function	benzaldehyde dehydrogenase (NAD+) activity
B	0019841	molecular_function	retinol binding
B	0042572	biological_process	retinol metabolic process
B	0046164	biological_process	alcohol catabolic process
B	0046294	biological_process	formaldehyde catabolic process
B	0046872	molecular_function	metal ion binding
B	0051287	molecular_function	NAD binding
B	0051903	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
B	1901661	biological_process	quinone metabolic process
C	0001523	biological_process	retinoid metabolic process
C	0003960	molecular_function	quinone reductase (NADPH) activity
C	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
C	0004032	molecular_function	aldose reductase (NADPH) activity
C	0004745	molecular_function	all-trans-retinol dehydrogenase (NAD+) activity
C	0005503	molecular_function	all-trans retinal binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006066	biological_process	alcohol metabolic process
C	0006081	biological_process	aldehyde metabolic process
C	0006629	biological_process	lipid metabolic process
C	0008270	molecular_function	zinc ion binding
C	0010430	biological_process	fatty acid omega-oxidation
C	0016491	molecular_function	oxidoreductase activity
C	0018479	molecular_function	benzaldehyde dehydrogenase (NAD+) activity
C	0019841	molecular_function	retinol binding
C	0042572	biological_process	retinol metabolic process
C	0046164	biological_process	alcohol catabolic process
C	0046294	biological_process	formaldehyde catabolic process
C	0046872	molecular_function	metal ion binding
C	0051287	molecular_function	NAD binding
C	0051903	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
C	1901661	biological_process	quinone metabolic process
D	0001523	biological_process	retinoid metabolic process
D	0003960	molecular_function	quinone reductase (NADPH) activity
D	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
D	0004032	molecular_function	aldose reductase (NADPH) activity
D	0004745	molecular_function	all-trans-retinol dehydrogenase (NAD+) activity
D	0005503	molecular_function	all-trans retinal binding
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006066	biological_process	alcohol metabolic process
D	0006081	biological_process	aldehyde metabolic process
D	0006629	biological_process	lipid metabolic process
D	0008270	molecular_function	zinc ion binding
D	0010430	biological_process	fatty acid omega-oxidation
D	0016491	molecular_function	oxidoreductase activity
D	0018479	molecular_function	benzaldehyde dehydrogenase (NAD+) activity
D	0019841	molecular_function	retinol binding
D	0042572	biological_process	retinol metabolic process
D	0046164	biological_process	alcohol catabolic process
D	0046294	biological_process	formaldehyde catabolic process
D	0046872	molecular_function	metal ion binding
D	0051287	molecular_function	NAD binding
D	0051903	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
D	1901661	biological_process	quinone metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	CYS47
A	HIS69
A	CYS180

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 502

Chain	Residue
A	CYS99
A	CYS102
A	CYS105
A	CYS113

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 501

Chain	Residue
B	CYS180
B	CYS47
B	HIS69

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 502

Chain	Residue
B	CYS99
B	CYS102
B	CYS105
B	CYS113

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 501

Chain	Residue
C	CYS47
C	HIS69
C	CYS180

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 502

Chain	Residue
C	CYS99
C	CYS102
C	CYS105
C	CYS113

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN D 501

Chain	Residue
D	CYS47
D	HIS69
D	CYS180

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 502

Chain	Residue
D	CYS99
D	CYS102
D	CYS105
D	CYS113

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAD A 400

Chain	Residue
A	HIS48
A	THR49
A	CYS180
A	THR184
A	GLY205
A	GLY207
A	GLY208
A	ASP229
A	LYS234
A	CYS274
A	ALA275
A	THR280
A	ILE298
A	GLY299
A	THR323
A	PHE324
A	PHE325
A	ARG375

site_id	BC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAD B 400

Chain	Residue
B	HIS48
B	THR49
B	CYS180
B	THR184
B	GLY205
B	GLY207
B	GLY208
B	ASP229
B	LYS234
B	CYS274
B	ALA275
B	THR280
B	ILE298
B	GLY299
B	THR323
B	PHE324
B	PHE325
B	ARG375

site_id	BC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD C 400

Chain	Residue
C	HIS48
C	THR49
C	CYS180
C	THR184
C	GLY205
C	GLY207
C	GLY208
C	ASP229
C	ILE230
C	LYS234
C	CYS274
C	ALA275
C	THR280
C	ILE298
C	GLY299
C	THR323
C	PHE324
C	PHE325
C	ARG375

site_id	BC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD D 400

Chain	Residue
D	THR323
D	PHE324
D	PHE325
D	ARG375
D	HIS48
D	THR49
D	CYS180
D	THR184
D	GLY205
D	GLY207
D	GLY208
D	ILE228
D	ASP229
D	ILE230
D	LYS234
D	CYS274
D	ALA275
D	THR280
D	ILE298
D	GLY299

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	SER124
A	ASP125
A	GLN126
A	GLN127
A	LEU128

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 503

Chain	Residue
B	PHE204
B	ILE228
B	PRO249

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 504

Chain	Residue
B	SER124
B	ASP125
B	GLN126
B	GLN127
B	LEU128

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 503

Chain	Residue
D	SER124
D	ASP125
D	GLN126
D	GLN127
D	LEU128

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 504

Chain	Residue
A	PHE204
A	PRO249
A	ILE256
A	ALA283

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 503

Chain	Residue
C	PHE204
C	PRO249

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 504

Chain	Residue
D	PHE204
D	ILE228
D	PRO249

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY A 401

Chain	Residue
A	CYS47
A	THR49
A	HIS69
A	TYR95
A	PHE147
A	CYS180

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY B 401

Chain	Residue
B	THR49
B	HIS69
B	TYR95
B	PHE147
B	CYS180

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY C 401

Chain	Residue
C	THR49
C	HIS69
C	TYR95
C	PHE147
C	CYS180

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY D 401

Chain	Residue
D	CYS47
D	THR49
D	HIS69
D	TYR95
D	PHE147
D	CYS180

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY B 505

Chain	Residue
A	SER304
B	GLU312

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY68-VAL82

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of human class II alcohol dehydrogenase (ADH4) in complex with NAD and Zn.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1teh

Chain	Residue	Details
A	HIS48
A	THR49

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1teh

Chain	Residue	Details
B	HIS48
B	THR49

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1teh

Chain	Residue	Details
C	HIS48
C	THR49

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

Chain	Residue	Details
D	HIS48
D	THR49

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

Chain	Residue	Details
A	PHE58

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

Chain	Residue	Details
B	PHE58

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

Chain	Residue	Details
C	PHE58

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

Chain	Residue	Details
D	PHE58

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