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1Y7T

Crystal structure of NAD(H)-depenent malate dehydrogenase complexed with NADPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006099biological_processtricarboxylic acid cycle
A0006107biological_processoxaloacetate metabolic process
A0006108biological_processmalate metabolic process
A0006734biological_processNADH metabolic process
A0016491molecular_functionoxidoreductase activity
A0016615molecular_functionmalate dehydrogenase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
A0030060molecular_functionL-malate dehydrogenase activity
B0003824molecular_functioncatalytic activity
B0006099biological_processtricarboxylic acid cycle
B0006107biological_processoxaloacetate metabolic process
B0006108biological_processmalate metabolic process
B0006734biological_processNADH metabolic process
B0016491molecular_functionoxidoreductase activity
B0016615molecular_functionmalate dehydrogenase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0030060molecular_functionL-malate dehydrogenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NDP A 1334
ChainResidue
ATHR9
AGLY87
AALA88
AGLN111
AGLY129
AASN130
ALEU157
ASER240
ASER241
AALA245
ATRS1335
AGLY10
ATRS1336
AHOH1369
AHOH1441
AHOH1454
AHOH1470
AHOH1497
AGLY13
AGLN14
AILE15
ALEU40
AGLU41
AILE42
AVAL86

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 1335
ChainResidue
AASN130
AGLY230
ASER240
ANDP1334
AHOH1353
AHOH1366
BLYS220

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS A 1336
ChainResidue
AASN130
ALEU157
AASP158
AARG161
AHIS186
ANDP1334
AHOH1366
AHOH1382
AHOH1386
AHOH1394

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NDP B 2334
ChainResidue
ALYS220
BTHR9
BGLY10
BGLY13
BGLN14
BILE15
BLEU40
BGLU41
BILE42
BVAL86
BGLY87
BALA88
BGLN111
BGLY129
BASN130
BLEU157
BSER240
BSER241
BALA245
BTRS2335
BTRS2336
BHOH2363
BHOH2455
BHOH2474
BHOH2496
BHOH2515
BHOH2532
BHOH2540

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS B 2335
ChainResidue
ALYS220
AHOH1510
BASN130
BGLY230
BSER240
BNDP2334
BHOH2362
BHOH2368
BHOH2504

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS B 2336
ChainResidue
BASN130
BLEU157
BASP158
BARG161
BHIS186
BNDP2334
BHOH2341
BHOH2362
BHOH2420
BHOH2422
BHOH2424

Functional Information from PROSITE/UniProt
site_idPS00068
Number of Residues13
DetailsMDH Malate dehydrogenase active site signature. MTRLDhnRAkaqL
ChainResidueDetails
AMET154-LEU166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01517
ChainResidueDetails
AHIS186
BHIS186

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341, ECO:0000269|PubMed:8471603
ChainResidueDetails
BGLY10
BVAL128
AGLY10
AVAL128

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517
ChainResidueDetails
AARG91
AARG97
BASN130
BARG161
AASN104
AASN130
AARG161
BARG91
BARG97
BASN104

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341
ChainResidueDetails
AGLN111
BGLN111

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PDB entries from 2024-05-29

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