Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ZTL

Closed conformation of D-3-hydroxybutyrate dehydrogenase complexed with NAD+ and L-3-hydroxybutyrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003858	molecular_function	3-hydroxybutyrate dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0032787	biological_process	monocarboxylic acid metabolic process
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0003858	molecular_function	3-hydroxybutyrate dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0032787	biological_process	monocarboxylic acid metabolic process
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0003858	molecular_function	3-hydroxybutyrate dehydrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0032787	biological_process	monocarboxylic acid metabolic process
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0003858	molecular_function	3-hydroxybutyrate dehydrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0032787	biological_process	monocarboxylic acid metabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD A 300

Chain	Residue
A	GLY11
A	ASP63
A	LEU64
A	ASN90
A	GLY92
A	LEU113
A	ILE140
A	ALA141
A	TYR155
A	LYS159
A	PRO185
A	THR13
A	GLY186
A	TRP187
A	VAL188
A	THR190
A	PRO191
A	LEU192
A	VAL193
A	3HL301
A	HOH1041
A	HOH1216
A	SER14
A	HOH1253
A	HOH1401
A	HOH1783
A	GLY15
A	ILE16
A	ASN34
A	GLY35
A	PHE36
A	ALA62

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 3HL A 301

Chain	Residue
A	GLN94
A	SER142
A	HIS144
A	LYS152
A	TYR155
A	TRP187
A	LEU192
A	GLN196
A	NAD300

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 406

Chain	Residue
A	ARG260
A	HOH410
D	ARG260
D	HOH407
D	HOH408
D	HOH409

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD B 300

Chain	Residue
B	GLY11
B	THR13
B	SER14
B	ILE16
B	ASN34
B	GLY35
B	PHE36
B	ALA62
B	ASP63
B	LEU64
B	ASN90
B	GLY92
B	LEU113
B	ILE140
B	ALA141
B	TYR155
B	LYS159
B	PRO185
B	GLY186
B	TRP187
B	VAL188
B	THR190
B	PRO191
B	VAL193
B	3HL301
B	HOH1169
B	HOH1766

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3HL B 301

Chain	Residue
B	GLN94
B	SER142
B	HIS144
B	LYS152
B	TYR155
B	LEU192
B	GLN196
B	NAD300

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 401

Chain	Residue
B	ARG260
B	HOH402
B	HOH405
C	ARG260
C	HOH403
C	HOH404

site_id	AC7
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAD C 300

Chain	Residue
C	ASN90
C	GLY92
C	LEU113
C	ILE140
C	ALA141
C	TYR155
C	LYS159
C	PRO185
C	GLY186
C	TRP187
C	VAL188
C	THR190
C	PRO191
C	LEU192
C	VAL193
C	3HL301
C	HOH1024
C	HOH1091
C	HOH1301
C	HOH1313
C	HOH1433
C	HOH1640
C	GLY11
C	THR13
C	SER14
C	GLY15
C	ILE16
C	ASN34
C	GLY35
C	PHE36
C	ALA62
C	ASP63
C	LEU64

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 3HL C 301

Chain	Residue
C	GLN94
C	SER142
C	HIS144
C	LYS152
C	TYR155
C	TRP187
C	LEU192
C	GLN196
C	NAD300

site_id	AC9
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAD D 300

Chain	Residue
D	GLY11
D	THR13
D	SER14
D	GLY15
D	ILE16
D	ASN34
D	GLY35
D	PHE36
D	ALA62
D	ASP63
D	LEU64
D	SER65
D	ASN90
D	GLY92
D	LEU113
D	ILE140
D	ALA141
D	TYR155
D	LYS159
D	PRO185
D	GLY186
D	TRP187
D	VAL188
D	THR190
D	PRO191
D	LEU192
D	VAL193
D	3HL301
D	HOH1036
D	HOH1068
D	HOH1226
D	HOH1406
D	HOH1614
D	HOH1792

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3HL D 301

Chain	Residue
D	GLN94
D	SER142
D	HIS144
D	LYS152
D	TYR155
D	LEU192
D	GLN196
D	NAD300

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL D 902

Chain	Residue
C	LYS3
C	LYS5
C	ARG83
C	HOH1103
C	HOH1803
D	TYR59
D	GLY61
D	HOH1100
D	HOH1292
D	HOH1335

Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. SahglvasanKsaYVAAKHGVvGFTkVTA

Chain	Residue	Details
A	SER142-ALA170

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
A	TYR155
A	SER142
A	ASN114
A	LYS159

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
B	TYR155
B	LYS159

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	TYR155
C	LYS159

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
D	TYR155
D	LYS159

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
B	TYR155
B	SER142
B	ASN114
B	LYS159

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	TYR155
C	SER142
C	ASN114
C	LYS159

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
D	TYR155
D	SER142
D	ASN114
D	LYS159

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
A	LYS152
A	LYS159

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
B	LYS152
B	LYS159

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	LYS152
C	LYS159

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
D	LYS152
D	LYS159

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
A	TYR155
A	LYS159

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