MolNFT v1 · #29666 · protein

Growth factor receptor binding protein SH2 domain complexed with a phosphotyrosyl pentapeptide

1ZFP: “Growth factor receptor binding protein SH2 domain complexed with a phosphotyrosyl pentapeptide”. X-ray diffraction, 3 ligands (BE2, ZN, NH2). MolNFT v1 #29666 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1ZFP
Type: protein
Length: 103 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Growth factor receptor binding protein; Epidermal growth factor receptor-derived peptide
UniProt: P29354
Ligands: BE2, ZN, NH2

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Growth factor receptor binding protein	protein	98	19% helix, 30% strand	P29354
I	Epidermal growth factor receptor-derived peptide	protein	5	0% helix, 0% strand	—

Ligands and binding sites

BE2 · 2-aminobenzoic acid · ligand · chains E, I
ZN · Zinc ion · metal · chains E
NH2 · Amino group · ion · chains I

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

Interfaces

1 interface between chains.

E–I · 422 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, phosphorylation).

Compared structures

1ZFP · Growth factor receptor binding protein SH2 domain complexed with a phosphotyrosyl… · the same entry in another collection · chain E against E, TM-score 1.00

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 P29354
Elsewhere: RCSB PDB 1ZFP · PDBe 1ZFP · UniProt P29354

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