Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I9H

Crystal structure of rabbit LDHA in complex with AP28669

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	22
Details	BINDING SITE FOR RESIDUE 1E4 A 401

Chain	Residue
A	GLY26
A	ASN114
A	ILE115
A	PHE118
A	VAL135
A	SER136
A	ASN137
A	ARG168
A	ALA237
A	THR247
A	HOH521
A	GLY28
A	HOH545
A	HOH551
A	HOH565
A	VAL30
A	ASP51
A	VAL52
A	THR94
A	ALA95
A	GLY96
A	ARG111

site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 1E4 B 401

Chain	Residue
B	VAL25
B	GLY26
B	GLY28
B	VAL30
B	ASP51
B	VAL52
B	THR94
B	ALA95
B	GLY96
B	ARG111
B	ILE115
B	PHE118
B	VAL135
B	SER136
B	ASN137
B	ARG168
B	ALA237
B	THR247
B	HOH501
B	HOH512

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 1E4 C 401

Chain	Residue
C	VAL25
C	GLY26
C	GLY28
C	VAL30
C	ASP51
C	VAL52
C	THR94
C	ALA95
C	GLY96
C	ARG111
C	ILE115
C	PHE118
C	VAL135
C	SER136
C	ASN137
C	ARG168
C	ALA237
C	THR247
C	HOH517
C	HOH525

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 1E4 D 401

Chain	Residue
D	GLY26
D	GLY28
D	VAL30
D	ASP51
D	VAL52
D	THR94
D	ALA95
D	GLY96
D	ARG111
D	ASN114
D	ILE115
D	PHE118
D	VAL135
D	SER136
D	ASN137
D	ARG168
D	ALA237
D	THR247
D	HOH520
D	HOH530
D	HOH545

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 1E4 E 401

Chain	Residue
E	SER136
E	ASN137
E	ARG168
E	ALA237
E	THR247
E	HOH504
E	HOH512
E	HOH530
E	VAL25
E	GLY26
E	GLY28
E	VAL30
E	VAL50
E	ASP51
E	VAL52
E	THR94
E	ALA95
E	GLY96
E	ARG98
E	ARG111
E	ILE115
E	PHE118
E	ILE119
E	VAL135

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 1E4 F 401

Chain	Residue
F	GLY26
F	GLY28
F	VAL30
F	ASP51
F	VAL52
F	THR94
F	ALA95
F	GLY96
F	ARG98
F	ARG111
F	ASN114
F	ILE115
F	PHE118
F	ILE119
F	VAL135
F	SER136
F	ASN137
F	LEU164
F	ARG168
F	ALA237
F	THR247

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 1E4 G 401

Chain	Residue
G	VAL25
G	GLY26
G	GLY28
G	VAL30
G	ASP51
G	VAL52
G	THR94
G	ALA95
G	GLY96
G	ARG111
G	ASN114
G	ILE115
G	PHE118
G	ILE119
G	VAL135
G	SER136
G	ASN137
G	LEU164
G	ARG168
G	ALA237
G	THR247
G	HOH521
G	HOH530
G	HOH552

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 1E4 H 401

Chain	Residue
H	VAL25
H	GLY26
H	GLY28
H	VAL30
H	ASP51
H	VAL52
H	THR94
H	ALA95
H	GLY96
H	ARG111
H	ASN114
H	ILE115
H	PHE118
H	VAL135
H	SER136
H	ASN137
H	ARG168
H	ALA237
H	THR247
H	HOH521
H	HOH534

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	262
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)