MolNFT v1 · #177406 · protein

Human MTHFD2 in complex with compound 21 and 9

7EHN: “Human MTHFD2 in complex with compound 21 and 9”. X-ray diffraction, 2 ligands (J4F, J49). MolNFT v1 #177406 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7EHN
Type: protein
Length: 566 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P13995
Ligands: J4F, J49

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	282	—	P13995
B	—	protein	284	—	P13995

Ligands and binding sites

J4F · 3-[4-[[1-[(4-chloranyl-1H-indol-2-yl)methyl]-3,7-dimethyl-2,6-bis(oxidanylidene)purin-8-yl]amino]-6-methyl-pyrimidin-2-yl]propanoic acid · ligand · 2 copies · chains A, B
J49 · (2S)-2-[[4-[(4-azanyl-6-oxidanyl-pyrimidin-5-yl) carbamoylamino]phenyl]carbonylamino]pentanedioic acid · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7EHN · Human MTHFD2 in complex with compound 21 and 9 · the same entry in another collection · chain A against A, TM-score 1.00
P13995 · AlphaFold monomer V2.0 prediction for bifunctional methylenetetrahydrofolate… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P13995
Elsewhere: RCSB PDB 7EHN · PDBe 7EHN · UniProt P13995

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