MolNFT v1 · #17282 · protein

Mutations in the T1.5 loop of pectate lyase a

1OOC: “Mutations in the T1.5 loop of pectate lyase a”. X-ray diffraction, 5 pockets (best druggability 0.73). MolNFT v1 #17282 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1OOC
Type: protein
Length: 722 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pectate lyase a
EC: 4.2.2.2
UniProt: P29155
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pectate lyase a (EC 4.2.2.2)	protein	361	16% helix, 36% strand	P29155

Pockets

5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	764	0.73	0.78	67	empty
2	110	0.46	0.79	24	empty
3	148	0.41	0.74	29	empty
4	78	0.32	0.74	22	empty
5	62	0.28	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 403 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1OOC · Mutations in the T1.5 loop of pectate lyase A · the same entry in another collection · chain A against A, 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 P29155
Elsewhere: RCSB PDB 1OOC · PDBe 1OOC · UniProt P29155

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