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

6S4E

Structure of human MTHFD2 in complex with TH7299

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004477molecular_functionmethenyltetrahydrofolate cyclohydrolase activity
A0004487molecular_functionmethylenetetrahydrofolate dehydrogenase (NAD+) activity
A0004488molecular_functionmethylenetetrahydrofolate dehydrogenase (NADP+) activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0035999biological_processtetrahydrofolate interconversion
A0042301molecular_functionphosphate ion binding
A0046653biological_processtetrahydrofolate metabolic process
A0046655biological_processfolic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue 9L9 A 401
ChainResidue
ASER83
AILE276
AARG278
ALEU289
APRO309
AGLY310
AGLY313
APRO314
ANAD406
AHOH517
AHOH525
ATYR84
AHOH544
AHOH571
AHOH585
AHOH587
AASN87
ALYS88
AVAL131
AGLN132
ALEU133
AASP155
APHE157

site_idAC2
Number of Residues5
Detailsbinding site for residue PO4 A 402
ChainResidue
AARG201
AARG233
ANAD406
AHOH563
AHOH564

site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 403
ChainResidue
AARG90
ALEU167
AASP168
AHIS219
AGLU220

site_idAC4
Number of Residues4
Detailsbinding site for residue PO4 A 404
ChainResidue
ALEU173
ATRP181
AARG221
APRO222

site_idAC5
Number of Residues3
Detailsbinding site for residue PO4 A 405
ChainResidue
AILE160
AARG164
AHOH501

site_idAC6
Number of Residues23
Detailsbinding site for residue NAD A 406
ChainResidue
ATHR176
AARG201
ASER202
AASN204
AVAL205
AHIS232
AARG233
AALA253
AALA254
AGLY255
AILE256
AVAL274
AGLY275
AILE276
AASN277
ATHR316
A9L9401
APO4402
AHOH512
AHOH538
AHOH544
AHOH557
AHOH563

Functional Information from PROSITE/UniProt
site_idPS00766
Number of Residues26
DetailsTHF_DHG_CYH_1 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 1. EeELLnlInkLNnDdnvdgLLVQLPL
ChainResidueDetails
AGLU110-LEU135

site_idPS00767
Number of Residues9
DetailsTHF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPMTV
ChainResidueDetails
APRO309-VAL317

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27899380
ChainResidueDetails
ATYR84
AVAL131
APRO309

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16100107, ECO:0000269|PubMed:27899380
ChainResidueDetails
AGLY200
AARG233

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS50

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS50

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon