Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6ECR

The human methylenetetrahydrofolate dehydrogenase/cyclohydrolase (FolD) complexed with NADP

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 Residues18
Detailsbinding site for residue NAP A 301
ChainResidue
ATHR148
AGLN218
ACYS236
AGLY237
AILE238
ATHR279
AHOH405
AHOH408
AHOH418
AHOH442
AARG173
ASER174
AVAL177
AHIS196
ASER197
AALA215
ATHR216
AGLY217

site_idAC2
Number of Residues24
Detailsbinding site for residue NAP B 301
ChainResidue
BTHR148
BGLY172
BARG173
BSER174
BVAL177
BHIS196
BSER197
BALA215
BTHR216
BGLY217
BGLN218
BMET221
BCYS236
BGLY237
BILE238
BTHR279
BHOH413
BHOH414
BHOH427
BHOH438
BHOH453
BHOH463
BHOH484
BHOH494

site_idAC3
Number of Residues6
Detailsbinding site for residue ACT B 302
ChainResidue
AGLY160
APRO162
BGLN23
BGLU289
BLYS292
BHOH406

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
BLYS56

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
BTYR52
BVAL99
BPRO272

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
BGLY172
BSER197

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
BMET1

Catalytic Information from CSA
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
BLYS56activator
BGLN100activator
BASP125electrostatic stabiliser

site_idMCSA4
Number of Residues3
DetailsM-CSA 458
ChainResidueDetails
BSER49activator
BLYS56proton shuttle (general acid/base)
BGLN100activator

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon