3UKO

Crystal Structure of S-Nitrosoglutathione Reductase from Arabidopsis thaliana, complex with NADH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
A	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0009536	cellular_component	plastid
A	0010286	biological_process	heat acclimation
A	0012501	biological_process	programmed cell death
A	0016491	molecular_function	oxidoreductase activity
A	0044281	biological_process	small molecule metabolic process
A	0046292	biological_process	formaldehyde metabolic process
A	0046294	biological_process	formaldehyde catabolic process
A	0046872	molecular_function	metal ion binding
A	0048316	biological_process	seed development
A	0051903	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
A	0080007	molecular_function	S-nitrosoglutathione reductase (NADH) activity
A	0106321	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
A	0106322	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
B	0004022	molecular_function	alcohol dehydrogenase (NAD+) activity
B	0005737	cellular_component	cytoplasm
B	0005777	cellular_component	peroxisome
B	0005829	cellular_component	cytosol
B	0008270	molecular_function	zinc ion binding
B	0009536	cellular_component	plastid
B	0010286	biological_process	heat acclimation
B	0012501	biological_process	programmed cell death
B	0016491	molecular_function	oxidoreductase activity
B	0044281	biological_process	small molecule metabolic process
B	0046292	biological_process	formaldehyde metabolic process
B	0046294	biological_process	formaldehyde catabolic process
B	0046872	molecular_function	metal ion binding
B	0048316	biological_process	seed development
B	0051903	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
B	0080007	molecular_function	S-nitrosoglutathione reductase (NADH) activity
B	0106321	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
B	0106322	molecular_function	S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 400

Chain	Residue
A	CYS99
A	CYS102
A	CYS105
A	CYS113

---

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

Chain	Residue
A	CYS47
A	HIS69
A	GLU70
A	CYS177

---

site_id	AC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD A 402

Chain	Residue
A	TYR95
A	THR181
A	GLY202
A	GLY204
A	THR205
A	VAL206
A	ASP226
A	ILE227
A	LYS231
A	CYS271
A	ILE272
A	VAL277
A	VAL295
A	GLY296
A	VAL297
A	THR320
A	ALA321
A	PHE322
A	ARG372
A	HOH395
A	HOH404
A	HOH460
A	HOH480
A	HOH493
A	HOH500
A	HOH555
A	HOH593
A	HOH631
A	HOH644
A	HIS48

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 1

Chain	Residue
A	VAL316
A	LYS318
A	HOH452
A	HOH505
A	HOH578
B	VAL316
B	LYS318

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 380

Chain	Residue
A	SER276
A	ARG279
A	HOH399
A	HOH524

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 381

Chain	Residue
A	HIS249
A	ASP250
A	LYS251

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 382

Chain	Residue
A	CYS102
A	LYS103
A	HOH442

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 383

Chain	Residue
A	ARG307
A	PHE309
A	HOH396
A	HOH470
B	SER300
B	GLY301

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 384

Chain	Residue
A	LYS287
A	HOH583
A	HOH648

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 385

Chain	Residue
A	ARG117
B	LYS287
B	PHE309
B	THR313
B	HOH386

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 400

Chain	Residue
B	CYS99
B	CYS102
B	CYS105
B	CYS113

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 401

Chain	Residue
B	CYS47
B	HIS69
B	GLU70
B	CYS177

---

site_id	BC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD B 402

Chain	Residue
B	HOH422
B	HOH435
B	HOH449
B	HOH500
B	HOH521
B	HOH541
B	HOH597
B	HOH631
B	HOH674
B	HIS48
B	TYR95
B	CYS177
B	THR181
B	GLY202
B	GLY204
B	THR205
B	VAL206
B	ASP226
B	ILE227
B	LYS231
B	CYS271
B	ILE272
B	VAL277
B	VAL295
B	GLY296
B	VAL297
B	THR320
B	ALA321
B	PHE322
B	ARG372
B	HOH385

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 380

Chain	Residue
B	HIS249
B	ASP250
B	LYS251

---

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 381

Chain	Residue
B	SER276
B	ARG279
B	SER305
B	HOH423

---

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 382

Chain	Residue
B	TYR43
B	PRO168
B	LEU169
B	ASP170
B	HOH613

---

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 383

Chain	Residue
B	ASN197
B	ARG221
B	TRP333
B	HOH468
B	HOH469
B	HOH534
B	HOH590
B	HOH647

---

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 384

Chain	Residue
B	CYS102
B	LYS103

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY68-VAL82

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"38308388","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure and kinetic behavior of alcohol dehydrogenase III /S-nitrosoglutathione reductase from arabidopsis thaliana.","authors":["Crotty J.","Greving M.","Brettschneider S.","Weichsel A.","Wildner G.F.","Vierling E.","Montfort W.R."]}},{"source":"PDB","id":"3UKO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GL4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L0Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CO4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	26
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure and kinetic behavior of alcohol dehydrogenase III /S-nitrosoglutathione reductase from arabidopsis thaliana.","authors":["Crotty J.","Greving M.","Brettschneider S.","Weichsel A.","Wildner G.F.","Vierling E.","Montfort W.R."]}},{"source":"PDB","id":"3UKO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GL4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L0Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P06525","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure and kinetic behavior of alcohol dehydrogenase III /S-nitrosoglutathione reductase from arabidopsis thaliana.","authors":["Crotty J.","Greving M.","Brettschneider S.","Weichsel A.","Wildner G.F.","Vierling E.","Montfort W.R."]}},{"source":"PDB","id":"3UKO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L0Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---