Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4KPW

Crystal structure of His-tagged human thymidylate synthase R175A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000900molecular_functionmRNA regulatory element binding translation repressor activity
A0004799molecular_functionthymidylate synthase activity
A0005542molecular_functionfolic acid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006231biological_processdTMP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0017148biological_processnegative regulation of translation
A0032259biological_processmethylation
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
A0071897biological_processDNA biosynthetic process
A1990825molecular_functionsequence-specific mRNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AARG50
AARG78
AARG176
AARG185
APRO305
ATHR306
AHOH607

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG215
ASER216
AASN183
AHIS196

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AGLU272
AARG274
AHIS304
AHOH550
AHOH583
AHOH609

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
AGLY29
AARG64
ATYR65
ASER66
AGLU70
APHE276

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 405
ChainResidue
AGLN36
AGLN62
AALA63
AVAL223
AHIS250
ALEU252
AHOH502

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 406
ChainResidue
AGLY217
AASP218
AGLY222
AASN226
AHOH524

Functional Information from PROSITE/UniProt
site_idPS00091
Number of Residues28
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RiiMca.WNprdlplma.....LpPCHalcQFyV
ChainResidueDetails
AARG176-VAL203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P45352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P45352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon