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4I9U

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

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 1E7 A 401
ChainResidue
AVAL25
APHE118
AILE119
AHOH535
AGLY26
AVAL50
AASP51
AVAL52
AALA95
AGLY96
AARG111
AILE115

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 1E7 B 401
ChainResidue
BVAL25
BGLY26
BVAL50
BASP51
BVAL52
BALA95
BARG111
BILE115
BPHE118
BILE119

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1E7 C 401
ChainResidue
CVAL25
CGLY26
CVAL50
CASP51
CVAL52
CALA95
CGLY96
CARG111
CILE115
CPHE118
CILE119

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1E7 D 401
ChainResidue
DVAL25
DGLY26
DVAL50
DASP51
DVAL52
DALA95
DGLY96
DARG111
DASN114
DILE115
DPHE118
DILE119

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 1E7 E 401
ChainResidue
EVAL25
EGLY26
EVAL50
EASP51
EVAL52
EARG98
EARG111
EILE115
EPHE118
EILE119

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1E7 F 401
ChainResidue
FVAL25
FGLY26
FVAL50
FASP51
FVAL52
FALA95
FGLY96
FARG98
FARG111
FILE115
FPHE118

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1E7 G 401
ChainResidue
GVAL25
GGLY26
GVAL50
GASP51
GVAL52
GALA95
GGLY96
GARG111
GILE115
GPHE118
GILE119
GHOH504

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1E7 H 401
ChainResidue
HVAL25
HGLY26
HVAL50
HASP51
HVAL52
HALA95
HGLY96
HARG111
HILE115
HPHE118
HHOH522

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
AHIS192
BHIS192
CHIS192
DHIS192
EHIS192
FHIS192
GHIS192
HHIS192

site_idSWS_FT_FI2
Number of Residues48
DetailsBINDING:
ChainResidueDetails
BARG105
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
AGLY28
AARG98
AARG105
AASN137
AARG168
ATHR247
BGLY28
BARG98

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

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

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

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

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

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

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

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00338
ChainResidueDetails
BSER309
CSER309
DSER309
ESER309
FSER309
GSER309
HSER309
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
ELYS56
FLYS56
GLYS56
HLYS56
ALYS56
BLYS56
CLYS56
DLYS56

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PDB entries from 2024-05-15

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