Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I9N

Crystal structure of rabbit LDHA in complex with AP28161 and AP28122

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 1E6 A 401

Chain	Residue
A	GLY26
A	ILE119
A	1E5402
A	HOH517
A	GLY28
A	ASP51
A	VAL52
A	THR94
A	ALA95
A	GLY96
A	ILE115
A	PHE118

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1E5 A 402

Chain	Residue
A	GLY28
A	ALA29
A	VAL30
A	THR94
A	VAL135
A	SER136
A	ASN137
A	ARG168
A	ALA237
A	THR247
A	1E6401
A	HOH509
A	HOH518
A	HOH546

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1E6 B 401

Chain	Residue
B	GLY26
B	GLY28
B	ASP51
B	VAL52
B	THR94
B	ALA95
B	GLY96
B	ARG111
B	ILE115
B	PHE118
B	ILE119
B	1E5402

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 1E5 B 402

Chain	Residue
B	GLY28
B	ALA29
B	VAL30
B	THR94
B	VAL135
B	SER136
B	ASN137
B	LEU164
B	ARG168
B	ALA237
B	THR247
B	1E6401
B	HOH520
B	HOH529
B	HOH532

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 1E6 C 401

Chain	Residue
C	GLY26
C	GLY28
C	ASP51
C	VAL52
C	THR94
C	ALA95
C	GLY96
C	ARG111
C	ILE115
C	PHE118
C	ILE119
C	1E5402
C	HOH534

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 1E5 C 402

Chain	Residue
C	GLY28
C	ALA29
C	VAL30
C	THR94
C	VAL135
C	SER136
C	ASN137
C	ARG168
C	ALA237
C	THR247
C	1E6401
C	HOH510
C	HOH512

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 1E6 D 401

Chain	Residue
D	GLY28
D	ASP51
D	VAL52
D	THR94
D	ALA95
D	GLY96
D	ARG111
D	ASN114
D	ILE115
D	PHE118
D	ILE119
D	1E5402
D	HOH535

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1E5 D 402

Chain	Residue
D	LEU164
D	ARG168
D	ALA237
D	THR247
D	1E6401
D	HOH510
D	HOH519
D	GLY28
D	ALA29
D	VAL30
D	THR94
D	VAL135
D	SER136
D	ASN137

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1E6 E 401

Chain	Residue
E	GLY26
E	GLY28
E	ASP51
E	VAL52
E	THR94
E	ALA95
E	GLY96
E	ARG98
E	ARG111
E	ASN114
E	ILE115
E	PHE118
E	ILE119
E	1E5402

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 1E5 E 402

Chain	Residue
E	GLY28
E	ALA29
E	VAL30
E	THR94
E	VAL135
E	SER136
E	ASN137
E	ARG168
E	ALA237
E	THR247
E	1E6401
E	HOH506
E	HOH515

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 1E6 F 401

Chain	Residue
F	GLY26
F	VAL27
F	GLY28
F	ASP51
F	VAL52
F	THR94
F	ALA95
F	GLY96
F	ARG98
F	ARG111
F	ASN114
F	ILE115
F	PHE118
F	1E5402
F	HOH508

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1E5 F 402

Chain	Residue
F	GLY28
F	ALA29
F	VAL30
F	THR94
F	VAL135
F	SER136
F	ASN137
F	ARG168
F	ALA237
F	THR247
F	1E6401
F	HOH509

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1E6 G 401

Chain	Residue
G	VAL25
G	GLY26
G	GLY28
G	ASP51
G	VAL52
G	THR94
G	ALA95
G	GLY96
G	ARG111
G	ILE115
G	PHE118
G	ILE119
G	1E5402
G	HOH522

site_id	BC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 1E5 G 402

Chain	Residue
G	GLY28
G	VAL30
G	THR94
G	VAL135
G	SER136
G	ASN137
G	LEU164
G	ARG168
G	ALA237
G	THR247
G	1E6401
G	HOH511
G	HOH539

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1E6 H 401

Chain	Residue
H	GLY26
H	GLY28
H	ASP51
H	VAL52
H	THR94
H	ALA95
H	GLY96
H	ARG111
H	ILE115
H	PHE118
H	ILE119
H	1E5402

site_id	BC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 1E5 H 402

Chain	Residue
H	GLY28
H	ALA29
H	VAL30
H	THR94
H	VAL135
H	SER136
H	ASN137
H	ARG168
H	ALA237
H	THR247
H	1E6401
H	HOH513
H	HOH527

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)