Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I9U

Crystal structure of rabbit LDHA in complex with a fragment inhibitor AP26256

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
A	0005737	cellular_component	cytoplasm
A	0006089	biological_process	lactate metabolic process
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
B	0003824	molecular_function	catalytic activity
B	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
B	0005737	cellular_component	cytoplasm
B	0006089	biological_process	lactate metabolic process
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
C	0003824	molecular_function	catalytic activity
C	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
C	0005737	cellular_component	cytoplasm
C	0006089	biological_process	lactate metabolic process
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
D	0003824	molecular_function	catalytic activity
D	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
D	0005737	cellular_component	cytoplasm
D	0006089	biological_process	lactate metabolic process
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
E	0003824	molecular_function	catalytic activity
E	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
E	0005737	cellular_component	cytoplasm
E	0006089	biological_process	lactate metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0019752	biological_process	carboxylic acid metabolic process
F	0003824	molecular_function	catalytic activity
F	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
F	0005737	cellular_component	cytoplasm
F	0006089	biological_process	lactate metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0019752	biological_process	carboxylic acid metabolic process
G	0003824	molecular_function	catalytic activity
G	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
G	0005737	cellular_component	cytoplasm
G	0006089	biological_process	lactate metabolic process
G	0016491	molecular_function	oxidoreductase activity
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0019752	biological_process	carboxylic acid metabolic process
H	0003824	molecular_function	catalytic activity
H	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
H	0005737	cellular_component	cytoplasm
H	0006089	biological_process	lactate metabolic process
H	0016491	molecular_function	oxidoreductase activity
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0019752	biological_process	carboxylic acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1E7 A 401

Chain	Residue
A	VAL25
A	PHE118
A	ILE119
A	HOH535
A	GLY26
A	VAL50
A	ASP51
A	VAL52
A	ALA95
A	GLY96
A	ARG111
A	ILE115

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1E7 B 401

Chain	Residue
B	VAL25
B	GLY26
B	VAL50
B	ASP51
B	VAL52
B	ALA95
B	ARG111
B	ILE115
B	PHE118
B	ILE119

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1E7 C 401

Chain	Residue
C	VAL25
C	GLY26
C	VAL50
C	ASP51
C	VAL52
C	ALA95
C	GLY96
C	ARG111
C	ILE115
C	PHE118
C	ILE119

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1E7 D 401

Chain	Residue
D	VAL25
D	GLY26
D	VAL50
D	ASP51
D	VAL52
D	ALA95
D	GLY96
D	ARG111
D	ASN114
D	ILE115
D	PHE118
D	ILE119

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1E7 E 401

Chain	Residue
E	VAL25
E	GLY26
E	VAL50
E	ASP51
E	VAL52
E	ARG98
E	ARG111
E	ILE115
E	PHE118
E	ILE119

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1E7 F 401

Chain	Residue
F	VAL25
F	GLY26
F	VAL50
F	ASP51
F	VAL52
F	ALA95
F	GLY96
F	ARG98
F	ARG111
F	ILE115
F	PHE118

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1E7 G 401

Chain	Residue
G	VAL25
G	GLY26
G	VAL50
G	ASP51
G	VAL52
G	ALA95
G	GLY96
G	ARG111
G	ILE115
G	PHE118
G	ILE119
G	HOH504

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1E7 H 401

Chain	Residue
H	VAL25
H	GLY26
H	VAL50
H	ASP51
H	VAL52
H	ALA95
H	GLY96
H	ARG111
H	ILE115
H	PHE118
H	HOH522

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	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19715328","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	261
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	24
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	16
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	16
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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