4L4S

Structural characterisation of the NADH binary complex of human lactate dehydrogenase M isozyme

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	0019661	biological_process	glucose catabolic process to lactate via pyruvate
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
A	1990204	cellular_component	oxidoreductase complex
H	0003824	molecular_function	catalytic activity
H	0004457	molecular_function	lactate dehydrogenase activity
H	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005739	cellular_component	mitochondrion
H	0005829	cellular_component	cytosol
H	0006089	biological_process	lactate metabolic process
H	0006096	biological_process	glycolytic process
H	0016020	cellular_component	membrane
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	0019661	biological_process	glucose catabolic process to lactate via pyruvate
H	0019752	biological_process	carboxylic acid metabolic process
H	0035686	cellular_component	sperm fibrous sheath
H	0042802	molecular_function	identical protein binding
H	0042867	biological_process	pyruvate catabolic process
H	0045296	molecular_function	cadherin binding
H	0070062	cellular_component	extracellular exosome
H	1990204	cellular_component	oxidoreductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAI H 401

Chain	Residue
H	GLY28
H	ARG98
H	ILE115
H	VAL135
H	SER136
H	ASN137
H	SER160
H	LEU164
H	HIS192
H	ILE251
H	HOH502
H	ALA29
H	VAL30
H	ASP51
H	VAL52
H	ILE53
H	THR94
H	ALA95
H	GLY96

---

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAI A 401

Chain	Residue
A	GLY28
A	ALA29
A	VAL30
A	ASP51
A	VAL52
A	ILE53
A	THR94
A	ALA95
A	GLY96
A	ILE115
A	VAL135
A	SER136
A	ASN137
A	SER160
A	LEU164
A	HIS192
A	ILE251
A	HOH506
A	HOH512

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
H	LEU189-SER195

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
H	HIS192
A	HIS192

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11276087

Chain	Residue	Details
H	GLY28
H	ARG98
A	GLY28
A	ARG98

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
H	ARG105
H	ASN137
H	ARG168
H	THR247
A	ARG105
A	ASN137
A	ARG168
A	THR247

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895

Chain	Residue	Details
H	ALA1
A	ALA1

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151

Chain	Residue	Details
H	LYS4
H	LYS117
H	LYS317
A	LYS4
A	LYS117
A	LYS317

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
H	TYR9
A	TYR9

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
H	LYS13
H	LYS80
H	LYS125
A	LYS13
A	LYS80
A	LYS125

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
H	THR17
A	THR17

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861

Chain	Residue	Details
H	LYS56
A	LYS56

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06151

Chain	Residue	Details
H	LYS223
H	LYS231
H	LYS242
A	LYS223
A	LYS231
A	LYS242

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06151

Chain	Residue	Details
H	TYR238
A	TYR238

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04642

Chain	Residue	Details
H	THR308
H	THR321
A	THR308
A	THR321

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
H	SER309
A	SER309

---

site_id	SWS_FT_FI14
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733

Chain	Residue	Details
H	LYS56
A	LYS56

---