Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ZXL

Structure of GldA from E.coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0008888	molecular_function	glycerol dehydrogenase (NAD+) activity
A	0015980	biological_process	energy derivation by oxidation of organic compounds
A	0016491	molecular_function	oxidoreductase activity
A	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
A	0019147	molecular_function	(R)-aminopropanol dehydrogenase activity
A	0019563	biological_process	glycerol catabolic process
A	0019588	biological_process	anaerobic glycerol catabolic process
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
A	0051596	biological_process	methylglyoxal catabolic process
B	0005829	cellular_component	cytosol
B	0008270	molecular_function	zinc ion binding
B	0008888	molecular_function	glycerol dehydrogenase (NAD+) activity
B	0015980	biological_process	energy derivation by oxidation of organic compounds
B	0016491	molecular_function	oxidoreductase activity
B	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
B	0019147	molecular_function	(R)-aminopropanol dehydrogenase activity
B	0019563	biological_process	glycerol catabolic process
B	0019588	biological_process	anaerobic glycerol catabolic process
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
B	0051596	biological_process	methylglyoxal catabolic process
C	0005829	cellular_component	cytosol
C	0008270	molecular_function	zinc ion binding
C	0008888	molecular_function	glycerol dehydrogenase (NAD+) activity
C	0015980	biological_process	energy derivation by oxidation of organic compounds
C	0016491	molecular_function	oxidoreductase activity
C	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
C	0019147	molecular_function	(R)-aminopropanol dehydrogenase activity
C	0019563	biological_process	glycerol catabolic process
C	0019588	biological_process	anaerobic glycerol catabolic process
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0051289	biological_process	protein homotetramerization
C	0051596	biological_process	methylglyoxal catabolic process
D	0005829	cellular_component	cytosol
D	0008270	molecular_function	zinc ion binding
D	0008888	molecular_function	glycerol dehydrogenase (NAD+) activity
D	0015980	biological_process	energy derivation by oxidation of organic compounds
D	0016491	molecular_function	oxidoreductase activity
D	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
D	0019147	molecular_function	(R)-aminopropanol dehydrogenase activity
D	0019563	biological_process	glycerol catabolic process
D	0019588	biological_process	anaerobic glycerol catabolic process
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0051289	biological_process	protein homotetramerization
D	0051596	biological_process	methylglyoxal catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 401

Chain	Residue
A	ASP121
A	ASP171
A	HIS254
A	HIS271
A	GOL402

site_id	AC2
Number of Residues	4
Details	binding site for residue GOL A 402

Chain	Residue
A	ASP121
A	PHE245
A	HIS254
A	ZN401

site_id	AC3
Number of Residues	1
Details	binding site for residue GOL A 403

Chain	Residue
A	ARG232

site_id	AC4
Number of Residues	5
Details	binding site for residue ZN B 401

Chain	Residue
B	ASP121
B	ASP171
B	HIS254
B	HIS271
B	GOL402

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL B 402

Chain	Residue
B	ASP121
B	PHE245
B	HIS254
B	HIS271
B	ZN401

site_id	AC6
Number of Residues	1
Details	binding site for residue GOL B 403

Chain	Residue
B	ARG232

site_id	AC7
Number of Residues	3
Details	binding site for residue GOL B 404

Chain	Residue
B	MET1
B	ARG3
D	GLY341

site_id	AC8
Number of Residues	1
Details	binding site for residue SO4 B 405

Chain	Residue
B	GLN311

site_id	AC9
Number of Residues	5
Details	binding site for residue ZN C 401

Chain	Residue
C	ASP121
C	ASP171
C	HIS254
C	HIS271
C	GOL402

site_id	AD1
Number of Residues	5
Details	binding site for residue GOL C 402

Chain	Residue
C	ASP121
C	PHE245
C	HIS254
C	HIS271
C	ZN401

site_id	AD2
Number of Residues	3
Details	binding site for residue GOL C 403

Chain	Residue
C	ARG232
D	ARG3
D	GLN197

site_id	AD3
Number of Residues	5
Details	binding site for residue GOL C 404

Chain	Residue
A	GLN347
C	MET1
C	ARG3
C	LYS194
D	GLU231

site_id	AD4
Number of Residues	1
Details	binding site for residue GOL C 405

Chain	Residue
C	ARG232

site_id	AD5
Number of Residues	1
Details	binding site for residue SO4 C 406

Chain	Residue
C	ARG184

site_id	AD6
Number of Residues	1
Details	binding site for residue SO4 C 407

Chain	Residue
C	GLN311

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN D 401

Chain	Residue
D	ASP171
D	HIS254
D	HIS271
D	GOL405

site_id	AD8
Number of Residues	2
Details	binding site for residue ZN D 402

Chain	Residue
D	HIS257
D	LYS274

site_id	AD9
Number of Residues	1
Details	binding site for residue GOL D 403

Chain	Residue
D	ARG232

site_id	AE1
Number of Residues	1
Details	binding site for residue GOL D 404

Chain	Residue
D	ARG31

site_id	AE2
Number of Residues	6
Details	binding site for residue GOL D 405

Chain	Residue
D	ASP121
D	ASP171
D	PHE245
D	HIS254
D	HIS271
D	ZN401

site_id	AE3
Number of Residues	1
Details	binding site for residue CL D 406

Chain	Residue
A	ASP54

site_id	AE4
Number of Residues	1
Details	binding site for residue SO4 D 407

Chain	Residue
D	GLN311

site_id	AE5
Number of Residues	3
Details	binding site for residue SO4 D 408

Chain	Residue
D	MET1
D	ARG3
D	LYS194

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER241-THR261

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. FESGGLAA

Chain	Residue	Details
A	PHE245-ALA252

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

Chain	Residue	Details
A	VAL150-GLU178

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P32816","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30839292","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZXL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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