Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4M49

Lactate Dehydrogenase A in complex with a substituted pyrazine inhibitor compound 18

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004457	molecular_function	lactate dehydrogenase activity
A	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006089	biological_process	lactate metabolic process
A	0006096	biological_process	glycolytic process
A	0016020	cellular_component	membrane
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	0019752	biological_process	carboxylic acid metabolic process
A	0035686	cellular_component	sperm fibrous sheath
A	0042802	molecular_function	identical protein binding
A	0042867	biological_process	pyruvate catabolic process
A	0045296	molecular_function	cadherin binding
A	0070062	cellular_component	extracellular exosome
B	0003824	molecular_function	catalytic activity
B	0004457	molecular_function	lactate dehydrogenase activity
B	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006089	biological_process	lactate metabolic process
B	0006096	biological_process	glycolytic process
B	0016020	cellular_component	membrane
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	0019752	biological_process	carboxylic acid metabolic process
B	0035686	cellular_component	sperm fibrous sheath
B	0042802	molecular_function	identical protein binding
B	0042867	biological_process	pyruvate catabolic process
B	0045296	molecular_function	cadherin binding
B	0070062	cellular_component	extracellular exosome
C	0003824	molecular_function	catalytic activity
C	0004457	molecular_function	lactate dehydrogenase activity
C	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006089	biological_process	lactate metabolic process
C	0006096	biological_process	glycolytic process
C	0016020	cellular_component	membrane
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	0019752	biological_process	carboxylic acid metabolic process
C	0035686	cellular_component	sperm fibrous sheath
C	0042802	molecular_function	identical protein binding
C	0042867	biological_process	pyruvate catabolic process
C	0045296	molecular_function	cadherin binding
C	0070062	cellular_component	extracellular exosome
D	0003824	molecular_function	catalytic activity
D	0004457	molecular_function	lactate dehydrogenase activity
D	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006089	biological_process	lactate metabolic process
D	0006096	biological_process	glycolytic process
D	0016020	cellular_component	membrane
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	0019752	biological_process	carboxylic acid metabolic process
D	0035686	cellular_component	sperm fibrous sheath
D	0042802	molecular_function	identical protein binding
D	0042867	biological_process	pyruvate catabolic process
D	0045296	molecular_function	cadherin binding
D	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAI A 801

Chain	Residue
A	GLY28
A	SER136
A	ASN137
A	SER160
A	HIS192
A	THR247
A	ILE251
A	22Y803
A	HOH904
A	HOH954
A	HOH970
A	ALA29
A	VAL30
A	ASP51
A	VAL52
A	ILE53
A	THR94
A	ALA95
A	VAL135

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EPE A 802

Chain	Residue
A	TRP147
A	GLY151
A	PHE152
A	PRO153
A	LYS154

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 22Y A 803

Chain	Residue
A	VAL30
A	ARG98
A	ASN137
A	HIS192
A	ILE241
A	GLY245
A	TYR246
A	THR247
A	NAI801
A	HOH1002

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 804

Chain	Residue
A	ARG170
A	HIS185
A	HOH917
A	HOH928
A	HOH969
C	LEU182
C	HIS185

site_id	AC5
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAI B 801

Chain	Residue
B	GLY28
B	ALA29
B	VAL30
B	ASP51
B	VAL52
B	ILE53
B	LYS56
B	THR94
B	ALA95
B	GLY96
B	ALA97
B	ARG98
B	GLN99
B	ILE115
B	ILE119
B	VAL135
B	ASN137
B	SER160
B	LEU164
B	HIS192
B	THR247
B	ILE251
B	LAC803
B	HOH901
B	HOH905
B	HOH909
B	HOH921
B	HOH948
B	HOH964
B	HOH982
B	HOH985

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE B 802

Chain	Residue
A	LYS283
B	TRP147
B	GLY151
B	PHE152
B	PRO153
B	LYS154
B	HOH1016
B	HOH1061

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE LAC B 803

Chain	Residue
B	GLN99
B	ARG105
B	ASN137
B	ARG168
B	HIS192
B	ALA237
B	THR247
B	NAI801

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NAI C 801

Chain	Residue
C	HIS192
C	THR247
C	22Y803
C	HOH921
C	GLY28
C	ALA29
C	VAL30
C	ASP51
C	VAL52
C	THR94
C	ALA95
C	ILE115
C	ILE119
C	VAL135
C	ASN137

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EPE C 802

Chain	Residue
C	TRP147
C	GLY151
C	PHE152
C	PRO153
C	LYS154

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 22Y C 803

Chain	Residue
C	ARG98
C	ASN137
C	HIS192
C	ILE241
C	GLY245
C	TYR246
C	THR247
C	NAI801

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 804

Chain	Residue
A	HIS185
A	HOH983
C	ARG170
C	HIS185
C	HOH913
C	HOH931
C	HOH933

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAI D 801

Chain	Residue
C	GLU101
D	GLY28
D	ALA29
D	VAL30
D	ASP51
D	VAL52
D	ILE53
D	THR94
D	ALA95
D	ARG98
D	ILE115
D	VAL135
D	ASN137
D	SER160
D	HIS192
D	22Y802
D	HOH905
D	HOH936
D	HOH983
D	HOH1034
D	HOH1036

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 22Y D 802

Chain	Residue
D	ARG98
D	ASN137
D	HIS192
D	ILE241
D	GLY245
D	TYR246
D	THR247
D	NAI801
D	HOH1034

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 803

Chain	Residue
B	LEU182
B	HIS185
D	ARG170
D	HIS185
D	HOH901
D	HOH915
D	HOH923

Functional Information from PROSITE/UniProt

site_id	PS00064
Number of Residues	7
Details	L_LDH L-lactate dehydrogenase active site. LGEHGDS

Chain	Residue	Details
A	LEU189-SER195

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	116
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11276087","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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