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The structure of the non-covalent complex of recombinant kringle 1 domain of human plasminogen with amcha (trans-4- aminomethylcyclohexane-1-carboxylic acid)

Analyse The structure of the non-covalent complex of recombinant kringle 1 domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CEB
Type: protein
Length: 160 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plasminogen
EC: 3.4.21.7
UniProt: P00747
Ligands: AMH

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Plasminogen (EC 3.4.21.7)	protein	80	4% helix, 16% strand	P00747

Ligands and binding sites

AMH · Trans-4-aminomethylcyclohexane-1-carboxylic acid · ligand · 2 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 189 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1CEB · The structure of the non-covalent complex of recombinant kringle 1 domain of human… · the same entry in another collection · chain A against A, TM-score 1.00
P00747 · AlphaFold monomer V2.0 prediction for plasminogen (P00747) · 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 P00747
Elsewhere: RCSB PDB 1CEB · PDBe 1CEB · UniProt P00747

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