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2XXB

Penta-mutant of Thermus thermophilus lactate dehydrogenase, complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0006096biological_processglycolytic 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 (NAD+) activity
B0005737cellular_componentcytoplasm
B0006089biological_processlactate metabolic process
B0006096biological_processglycolytic 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
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AMP A 1332
ChainResidue
AVAL27
AALA98
AGLY99
AVAL119
AVAL123
AHOH2135
AHOH2136
AHOH2137
AHOH2138
BGLY106
BGLN111
AGLY28
AGLY30
AMET31
AVAL32
AASP53
ALEU54
ALEU58
ATYR85

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AMP B 1332
ChainResidue
BGLY30
BMET31
BVAL32
BASP53
BLEU54
BLEU58
BTYR85
BALA98
BGLY99
BVAL123
BHOH2148
BHOH2149
BHOH2150
BHOH2151
BHOH2152
BHOH2153
BHOH2154

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. LGEHGDS
ChainResidueDetails
ALEU192-SER198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Structure of TT0471 protein from Thermus thermophilus.","authors":["Lokanath N.K.","Kunishima N."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PubMed","id":"22319152","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2E37","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZZN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

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