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1DIG

HUMAN METHYLENETETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE COMPLEXED WITH NADP AND INHIBITOR LY374571

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004488molecular_functionmethylenetetrahydrofolate dehydrogenase (NADP+) activity
B0003824molecular_functioncatalytic activity
B0004488molecular_functionmethylenetetrahydrofolate dehydrogenase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 4000
ChainResidue
APRO162
BGLN1023
BGLU1289
BLYS1292
BHOH4208

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAP A 2001
ChainResidue
ASER197
ALEU202
AALA215
ATHR216
AGLY217
AGLN218
AMET221
ACYS236
AILE238
AGLY276
ATHR279
AL373001
AHOH4011
AHOH4111
AHOH4112
AHOH4163
ATHR148
AARG173
ASER174
AHIS196

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAP B 2002
ChainResidue
BTHR1148
BGLY1172
BARG1173
BSER1174
BHIS1196
BSER1197
BALA1215
BTHR1216
BGLY1217
BGLN1218
BMET1221
BCYS1236
BILE1238
BGLY1276
BTHR1279
BHOH4025
BHOH4026
BHOH4087
BHOH4088
BHOH4107
BHOH4198
BHOH4201

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE L37 A 3001
ChainResidue
ALYS56
ALEU101
AILE238
AGLY273
AGLY274
AGLY276
APRO277
ANAP2001
AHOH4012

Functional Information from PROSITE/UniProt
site_idPS00766
Number of Residues26
DetailsTHF_DHG_CYH_1 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 1. EsEVMkyItsLNeDstvhgFLVQLPL
ChainResidueDetails
AGLU78-LEU103

site_idPS00767
Number of Residues9
DetailsTHF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPMTV
ChainResidueDetails
APRO272-VAL280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:10828945
ChainResidueDetails
ALYS56
BLYS1056

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB
ChainResidueDetails
ATYR52
AVAL99
APRO272
BTYR1052
BVAL1099
BPRO1272

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10828945, ECO:0000269|PubMed:9519408, ECO:0007744|PDB:1A4I, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB, ECO:0007744|PDB:1DIG
ChainResidueDetails
AGLY172
ASER197
BGLY1172
BSER1197

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1001

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a4i
ChainResidueDetails
ALYS56

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a4i
ChainResidueDetails
BLYS1056

site_idMCSA1
Number of Residues3
DetailsM-CSA 389
ChainResidueDetails
ALYS56activator
AGLN100activator
AASP125electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 458
ChainResidueDetails
ASER49activator
ALYS56proton shuttle (general acid/base)
AGLN100activator

site_idMCSA3
Number of Residues3
DetailsM-CSA 389
ChainResidueDetails
BLYS1056activator
BGLN1100activator
BASP1125electrostatic stabiliser

site_idMCSA4
Number of Residues3
DetailsM-CSA 458
ChainResidueDetails
BSER1049activator
BLYS1056proton shuttle (general acid/base)
BGLN1100activator

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PDB entries from 2024-07-17

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