Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1IB6

CRYSTAL STRUCTURE OF R153C E. COLI MALATE DEHYDROGENASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006096	biological_process	glycolytic process
A	0006099	biological_process	tricarboxylic acid cycle
A	0006108	biological_process	malate metabolic process
A	0009061	biological_process	anaerobic respiration
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016615	molecular_function	malate dehydrogenase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0019752	biological_process	carboxylic acid metabolic process
A	0019898	cellular_component	extrinsic component of membrane
A	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
A	0042803	molecular_function	protein homodimerization activity
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006096	biological_process	glycolytic process
B	0006099	biological_process	tricarboxylic acid cycle
B	0006108	biological_process	malate metabolic process
B	0009061	biological_process	anaerobic respiration
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0016615	molecular_function	malate dehydrogenase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0019752	biological_process	carboxylic acid metabolic process
B	0019898	cellular_component	extrinsic component of membrane
B	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
B	0042803	molecular_function	protein homodimerization activity
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006096	biological_process	glycolytic process
C	0006099	biological_process	tricarboxylic acid cycle
C	0006108	biological_process	malate metabolic process
C	0009061	biological_process	anaerobic respiration
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0016615	molecular_function	malate dehydrogenase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0019752	biological_process	carboxylic acid metabolic process
C	0019898	cellular_component	extrinsic component of membrane
C	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
C	0042803	molecular_function	protein homodimerization activity
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006096	biological_process	glycolytic process
D	0006099	biological_process	tricarboxylic acid cycle
D	0006108	biological_process	malate metabolic process
D	0009061	biological_process	anaerobic respiration
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0016615	molecular_function	malate dehydrogenase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0019752	biological_process	carboxylic acid metabolic process
D	0019898	cellular_component	extrinsic component of membrane
D	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
D	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 316

Chain	Residue
A	ARG81
A	ARG87
A	ASN119
A	HIS177
A	GLY210
A	NAD313
A	HOH344
A	HOH353

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 317

Chain	Residue
A	ASP86
A	ARG87
A	SER88
A	SER178
A	GLY179
A	ARG81

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 318

Chain	Residue
C	ARG81
C	ARG87
C	ASN119
C	HIS177
C	GLY210
C	NAD314
C	HOH473

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 319

Chain	Residue
C	ARG81
C	ASP86
C	ARG87
C	SER88
C	SER178
C	GLY179
C	HOH467

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 320

Chain	Residue
D	ARG81
D	ARG87
D	ASN119
D	HIS177
D	GLY210
D	NAD315
D	HOH531
D	HOH532
D	HOH533

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 321

Chain	Residue
D	ASP86
D	ARG87
D	SER88
D	SER178
D	GLY179

site_id	AC7
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD A 313

Chain	Residue
A	GLY7
A	ALA9
A	GLY10
A	GLY11
A	ILE12
A	TYR33
A	ASP34
A	ILE35
A	SER76
A	ALA77
A	GLY78
A	VAL79
A	ALA80
A	LEU90
A	ASN94
A	ILE97
A	ILE117
A	THR118
A	ASN119
A	VAL146
A	LEU149
A	HIS177
A	ALA223
A	MET227
A	SO4316
A	HOH343
A	HOH345
A	HOH348
A	HOH349
A	HOH396
A	HOH397

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD C 314

Chain	Residue
C	HOH479
C	HOH480
C	ALA9
C	GLY10
C	GLY11
C	ILE12
C	TYR33
C	ASP34
C	ILE35
C	SER76
C	ALA77
C	GLY78
C	VAL79
C	ALA80
C	ASN94
C	ILE97
C	ILE117
C	ASN119
C	VAL121
C	VAL146
C	HIS177
C	ALA223
C	THR224
C	MET227
C	SO4318
C	HOH473
C	HOH474
C	HOH475

site_id	AC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD D 315

Chain	Residue
D	GLY7
D	ALA9
D	GLY10
D	GLY11
D	ILE12
D	TYR33
D	ASP34
D	SER76
D	ALA77
D	GLY78
D	VAL79
D	LEU90
D	ASN94
D	ILE97
D	ILE117
D	ASN119
D	VAL121
D	VAL146
D	HIS177
D	ALA223
D	THR224
D	MET227
D	SO4320
D	HOH529
D	HOH530
D	HOH531
D	HOH549
D	HOH563
D	HOH564
D	HOH577

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1507230","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS177
A	ASP150

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

Chain	Residue	Details
B	HIS177
B	ASP150

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

Chain	Residue	Details
C	HIS177
C	ASP150

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

Chain	Residue	Details
D	HIS177
D	ASP150

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
A	HIS177
A	ASP150
A	CYS153

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
B	HIS177
B	ASP150
B	CYS153

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
C	HIS177
C	ASP150
C	CYS153

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
D	HIS177
D	ASP150
D	CYS153

site_id	MCSA1
Number of Residues	2
Details	M-CSA 527

Chain	Residue	Details
A	ASP150	modifies pKa
A	HIS177	proton acceptor, proton donor

site_id	MCSA2
Number of Residues	2
Details	M-CSA 527

Chain	Residue	Details
B	ASP150	modifies pKa
B	HIS177	proton acceptor, proton donor

site_id	MCSA3
Number of Residues	2
Details	M-CSA 527

Chain	Residue	Details
C	ASP150	modifies pKa
C	HIS177	proton acceptor, proton donor

site_id	MCSA4
Number of Residues	2
Details	M-CSA 527

Chain	Residue	Details
D	ASP150	modifies pKa
D	HIS177	proton acceptor, proton donor

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