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4I9N

Crystal structure of rabbit LDHA in complex with AP28161 and AP28122

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0006089biological_processlactate metabolic process
B0006090biological_processpyruvate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
C0003824molecular_functioncatalytic activity
C0004459molecular_functionL-lactate dehydrogenase activity
C0005737cellular_componentcytoplasm
C0006089biological_processlactate metabolic process
C0006090biological_processpyruvate metabolic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019752biological_processcarboxylic acid metabolic process
D0003824molecular_functioncatalytic activity
D0004459molecular_functionL-lactate dehydrogenase activity
D0005737cellular_componentcytoplasm
D0006089biological_processlactate metabolic process
D0006090biological_processpyruvate metabolic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019752biological_processcarboxylic acid metabolic process
E0003824molecular_functioncatalytic activity
E0004459molecular_functionL-lactate dehydrogenase activity
E0005737cellular_componentcytoplasm
E0006089biological_processlactate metabolic process
E0006090biological_processpyruvate metabolic process
E0016491molecular_functionoxidoreductase activity
E0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E0019752biological_processcarboxylic acid metabolic process
F0003824molecular_functioncatalytic activity
F0004459molecular_functionL-lactate dehydrogenase activity
F0005737cellular_componentcytoplasm
F0006089biological_processlactate metabolic process
F0006090biological_processpyruvate metabolic process
F0016491molecular_functionoxidoreductase activity
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0019752biological_processcarboxylic acid metabolic process
G0003824molecular_functioncatalytic activity
G0004459molecular_functionL-lactate dehydrogenase activity
G0005737cellular_componentcytoplasm
G0006089biological_processlactate metabolic process
G0006090biological_processpyruvate metabolic process
G0016491molecular_functionoxidoreductase activity
G0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G0019752biological_processcarboxylic acid metabolic process
H0003824molecular_functioncatalytic activity
H0004459molecular_functionL-lactate dehydrogenase activity
H0005737cellular_componentcytoplasm
H0006089biological_processlactate metabolic process
H0006090biological_processpyruvate metabolic process
H0016491molecular_functionoxidoreductase activity
H0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1E6 A 401
ChainResidue
AGLY26
AILE119
A1E5402
AHOH517
AGLY28
AASP51
AVAL52
ATHR94
AALA95
AGLY96
AILE115
APHE118

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1E5 A 402
ChainResidue
AGLY28
AALA29
AVAL30
ATHR94
AVAL135
ASER136
AASN137
AARG168
AALA237
ATHR247
A1E6401
AHOH509
AHOH518
AHOH546

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1E6 B 401
ChainResidue
BGLY26
BGLY28
BASP51
BVAL52
BTHR94
BALA95
BGLY96
BARG111
BILE115
BPHE118
BILE119
B1E5402

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 1E5 B 402
ChainResidue
BGLY28
BALA29
BVAL30
BTHR94
BVAL135
BSER136
BASN137
BLEU164
BARG168
BALA237
BTHR247
B1E6401
BHOH520
BHOH529
BHOH532

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1E6 C 401
ChainResidue
CGLY26
CGLY28
CASP51
CVAL52
CTHR94
CALA95
CGLY96
CARG111
CILE115
CPHE118
CILE119
C1E5402
CHOH534

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1E5 C 402
ChainResidue
CGLY28
CALA29
CVAL30
CTHR94
CVAL135
CSER136
CASN137
CARG168
CALA237
CTHR247
C1E6401
CHOH510
CHOH512

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1E6 D 401
ChainResidue
DGLY28
DASP51
DVAL52
DTHR94
DALA95
DGLY96
DARG111
DASN114
DILE115
DPHE118
DILE119
D1E5402
DHOH535

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1E5 D 402
ChainResidue
DLEU164
DARG168
DALA237
DTHR247
D1E6401
DHOH510
DHOH519
DGLY28
DALA29
DVAL30
DTHR94
DVAL135
DSER136
DASN137

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1E6 E 401
ChainResidue
EGLY26
EGLY28
EASP51
EVAL52
ETHR94
EALA95
EGLY96
EARG98
EARG111
EASN114
EILE115
EPHE118
EILE119
E1E5402

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1E5 E 402
ChainResidue
EGLY28
EALA29
EVAL30
ETHR94
EVAL135
ESER136
EASN137
EARG168
EALA237
ETHR247
E1E6401
EHOH506
EHOH515

site_idBC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 1E6 F 401
ChainResidue
FGLY26
FVAL27
FGLY28
FASP51
FVAL52
FTHR94
FALA95
FGLY96
FARG98
FARG111
FASN114
FILE115
FPHE118
F1E5402
FHOH508

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1E5 F 402
ChainResidue
FGLY28
FALA29
FVAL30
FTHR94
FVAL135
FSER136
FASN137
FARG168
FALA237
FTHR247
F1E6401
FHOH509

site_idBC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1E6 G 401
ChainResidue
GVAL25
GGLY26
GGLY28
GASP51
GVAL52
GTHR94
GALA95
GGLY96
GARG111
GILE115
GPHE118
GILE119
G1E5402
GHOH522

site_idBC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1E5 G 402
ChainResidue
GGLY28
GVAL30
GTHR94
GVAL135
GSER136
GASN137
GLEU164
GARG168
GALA237
GTHR247
G1E6401
GHOH511
GHOH539

site_idBC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1E6 H 401
ChainResidue
HGLY26
HGLY28
HASP51
HVAL52
HTHR94
HALA95
HGLY96
HARG111
HILE115
HPHE118
HILE119
H1E5402

site_idBC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1E5 H 402
ChainResidue
HGLY28
HALA29
HVAL30
HTHR94
HVAL135
HSER136
HASN137
HARG168
HALA237
HTHR247
H1E6401
HHOH513
HHOH527

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. LGEHGDS
ChainResidueDetails
ALEU189-SER195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:19715328
ChainResidueDetails
HHIS192
BHIS192
CHIS192
DHIS192
EHIS192
FHIS192
GHIS192
AHIS192

site_idSWS_FT_FI2
Number of Residues48
DetailsBINDING:
ChainResidueDetails
BASN137
BARG168
BTHR247
CGLY28
CARG98
CARG105
CASN137
CARG168
CTHR247
DGLY28
DARG98
DARG105
DASN137
DARG168
DTHR247
EGLY28
EARG98
EARG105
EASN137
EARG168
ETHR247
FGLY28
FARG98
FARG105
FASN137
FARG168
FTHR247
GGLY28
GARG98
GARG105
GASN137
GARG168
GTHR247
HGLY28
HARG98
HARG105
HASN137
HARG168
HTHR247
BARG104
AARG98
AARG105
AASN137
AARG168
ATHR247
BGLY28
BARG97
AGLY28

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P00338
ChainResidueDetails
BALA1
CALA1
DALA1
EALA1
FALA1
GALA1
HALA1
AALA1

site_idSWS_FT_FI4
Number of Residues24
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
ChainResidueDetails
DLYS4
DLYS117
DLYS317
ELYS4
ELYS117
ELYS317
FLYS4
FLYS117
FLYS317
GLYS4
GLYS117
GLYS317
HLYS4
HLYS117
HLYS317
BLYS4
BLYS117
BLYS317
CLYS4
CLYS117
CLYS317
ALYS4
ALYS117
ALYS317

site_idSWS_FT_FI5
Number of Residues24
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00338
ChainResidueDetails
DLYS13
DLYS80
DLYS125
ELYS13
ELYS80
ELYS125
FLYS13
FLYS80
FLYS125
GLYS13
GLYS80
GLYS125
HLYS13
HLYS80
HLYS125
CLYS125
ALYS80
ALYS125
BLYS13
BLYS80
BLYS125
CLYS13
CLYS80
ALYS13

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338
ChainResidueDetails
BLYS56
CLYS56
DLYS56
ELYS56
FLYS56
GLYS56
HLYS56
ALYS56

site_idSWS_FT_FI7
Number of Residues24
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06151
ChainResidueDetails
GLYS223
GLYS231
GLYS242
DLYS223
DLYS231
DLYS242
ELYS223
ELYS231
ELYS242
FLYS223
FLYS231
FLYS242
ALYS231
HLYS223
HLYS231
HLYS242
ALYS242
BLYS223
BLYS231
BLYS242
CLYS223
CLYS231
CLYS242
ALYS223

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06151
ChainResidueDetails
BTYR238
CTYR238
DTYR238
ETYR238
FTYR238
GTYR238
HTYR238
ATYR238

site_idSWS_FT_FI9
Number of Residues16
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04642
ChainResidueDetails
ETHR321
FTHR308
FTHR321
GTHR308
GTHR321
HTHR308
HTHR321
DTHR308
BTHR321
CTHR308
CTHR321
DTHR321
ETHR308
ATHR308
ATHR321
BTHR308

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00338
ChainResidueDetails
HSER309
BSER309
CSER309
DSER309
ESER309
FSER309
GSER309
ASER309

site_idSWS_FT_FI11
Number of Residues16
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P00338
ChainResidueDetails
FLYS56
GLYS56
HLYS56
BLYS56
CLYS56
DLYS56
ELYS56
ALYS56

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PDB entries from 2024-07-24

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