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Thermodynamic and structural consequences of changing a sulphur atom to a methylene group in the M13NLE mutation in ribonuclease S

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PDB: 2RLN
Type: protein
Length: 119 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease; Ribonuclease S (S-protein)
EC: 3.1.27.5
UniProt: P00656
Ligands: NH2, SO4

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
S	Ribonuclease	protein	15	60% helix, 7% strand	—
E	Ribonuclease S (S-protein) (EC 3.1.27.5)	protein	104	16% helix, 41% strand	P00656

Ligands and binding sites

NH2 · Amino group · ion · chains S
SO4 · Sulfate ion · ion · chains S, E

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

Interfaces

1 interface between chains.

S–E · 705 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 1 modified (disulfide, nonstandard).

Compared structures

2RLN · Thermodynamic and structural consequences of changing a sulphur atom to a methylene group… · the same entry in another collection · chain S against S, TM-score 1.00

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Every structure of UniProt P00656
Elsewhere: RCSB PDB 2RLN · PDBe 2RLN · UniProt P00656

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