Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OJ7

STRUCTURAL GENOMICS, UNKNOWN FUNCTION CRYSTAL STRUCTURE OF E. COLI K-12 YQHD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000302	biological_process	response to reactive oxygen species
A	0005829	cellular_component	cytosol
A	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
A	0008270	molecular_function	zinc ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0018455	molecular_function	alcohol dehydrogenase [NAD(P)+] activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0047655	molecular_function	allyl-alcohol dehydrogenase activity
A	1990002	molecular_function	methylglyoxal reductase (NADPH) (acetol producing) activity
A	1990362	molecular_function	butanol dehydrogenase (NAD+) activity
B	0000302	biological_process	response to reactive oxygen species
B	0005829	cellular_component	cytosol
B	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
B	0008270	molecular_function	zinc ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0018455	molecular_function	alcohol dehydrogenase [NAD(P)+] activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0047655	molecular_function	allyl-alcohol dehydrogenase activity
B	1990002	molecular_function	methylglyoxal reductase (NADPH) (acetol producing) activity
B	1990362	molecular_function	butanol dehydrogenase (NAD+) activity
C	0000302	biological_process	response to reactive oxygen species
C	0005829	cellular_component	cytosol
C	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
C	0008270	molecular_function	zinc ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0018455	molecular_function	alcohol dehydrogenase [NAD(P)+] activity
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0047655	molecular_function	allyl-alcohol dehydrogenase activity
C	1990002	molecular_function	methylglyoxal reductase (NADPH) (acetol producing) activity
C	1990362	molecular_function	butanol dehydrogenase (NAD+) activity
D	0000302	biological_process	response to reactive oxygen species
D	0005829	cellular_component	cytosol
D	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
D	0008270	molecular_function	zinc ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0018455	molecular_function	alcohol dehydrogenase [NAD(P)+] activity
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0047655	molecular_function	allyl-alcohol dehydrogenase activity
D	1990002	molecular_function	methylglyoxal reductase (NADPH) (acetol producing) activity
D	1990362	molecular_function	butanol dehydrogenase (NAD+) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B1389

Chain	Residue
B	ASP194
B	HIS198
B	HIS267
B	HIS281
B	NZQ1388

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C1388

Chain	Residue
C	BO31390
C	ASP194
C	HIS198
C	HIS267
C	HIS281

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C1389

Chain	Residue
C	GLY38
C	GLY39
C	SER40
C	HOH2031
C	HOH2064

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN D1389

Chain	Residue
D	ASP194
D	HIS198
D	HIS267
D	HIS281
D	LEU285
D	NZQ1388

site_id	AC5
Number of Residues	44
Details	BINDING SITE FOR RESIDUE NZQ A1388

Chain	Residue
A	GLY38
A	GLY39
A	SER40
A	PRO67
A	ASN68
A	GLY94
A	GLY95
A	SER96
A	ASP99
A	THR138
A	LEU139
A	ALA141
A	THR142
A	SER144
A	ASN147
A	GLY149
A	VAL151
A	LYS160
A	TYR179
A	THR182
A	LEU183
A	GLN187
A	ASP194
A	HIS198
A	HIS267
A	HIS271
A	HIS281
A	HOH2069
A	HOH2134
A	HOH2170
A	HOH2352
A	HOH2353
A	HOH2354
A	HOH2355
A	HOH2356
A	HOH2357
A	HOH2358
A	HOH2359
A	HOH2360
A	HOH2361
A	HOH2362
A	HOH2363
A	HOH2364
A	HOH2365

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BO3 A1389

Chain	Residue
A	ARG186
A	ASN190
A	ASP280
A	GLN283
A	GLY338
A	VAL339

site_id	AC7
Number of Residues	46
Details	BINDING SITE FOR RESIDUE NZQ B1388

Chain	Residue
B	HIS281
B	ZN1389
B	HOH2083
B	HOH2161
B	HOH2171
B	HOH2210
B	HOH2417
B	HOH2418
B	HOH2419
B	HOH2420
B	HOH2421
B	HOH2422
B	HOH2423
B	HOH2424
B	HOH2425
B	HOH2426
B	HOH2427
B	HOH2428
B	GLY38
B	GLY39
B	SER40
B	PRO67
B	ASN68
B	GLY94
B	GLY95
B	SER96
B	ASP99
B	THR138
B	LEU139
B	ALA141
B	THR142
B	SER144
B	ASN147
B	GLY149
B	VAL151
B	LYS160
B	TYR179
B	THR182
B	LEU183
B	PRO184
B	GLN187
B	ASP194
B	HIS198
B	LEU252
B	HIS267
B	HIS271

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BO3 C1390

Chain	Residue
C	ASP194
C	HIS198
C	HIS267
C	HIS281
C	ZN1388

site_id	AC9
Number of Residues	43
Details	BINDING SITE FOR RESIDUE NZQ D1388

Chain	Residue
D	GLY38
D	GLY39
D	SER40
D	PRO67
D	ASN68
D	GLY94
D	GLY95
D	SER96
D	ASP99
D	THR138
D	LEU139
D	ALA141
D	THR142
D	SER144
D	ASN147
D	GLY149
D	VAL151
D	LYS160
D	TYR179
D	THR182
D	LEU183
D	GLN187
D	ASP194
D	HIS198
D	HIS267
D	HIS271
D	HIS281
D	ZN1389
D	HOH2090
D	HOH2282
D	HOH2283
D	HOH2284
D	HOH2285
D	HOH2286
D	HOH2287
D	HOH2288
D	HOH2289
D	HOH2290
D	HOH2292
D	HOH2293
D	HOH2294
D	HOH2295
D	HOH2296

Functional Information from PROSITE/UniProt

site_id	PS00060
Number of Residues	21
Details	ADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. WaTHmlGHeLTAmhgLdHAqT

Chain	Residue	Details
A	TRP264-THR284

site_id	PS00913
Number of Residues	29
Details	ADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. AVlDpvytytlPprqvAnGvvDAFvhtvE

Chain	Residue	Details
A	ALA173-GLU201

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15327949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OJ7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15327949","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2014","submissionDatabase":"PDB data bank","title":"Open form of E. coli YqhD.","authors":["LaMattina J.W.","Kapoor S.","Gouvea I.","Slovic A.","Lanzilotta W.N."]}},{"source":"PDB","id":"1OJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QGS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS271

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

Chain	Residue	Details
B	HIS271

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

Chain	Residue	Details
C	HIS271

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

Chain	Residue	Details
D	HIS271

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