MolNFT v1 · #92973 · protein

Crystal structure of a DUF1491 family protein (CC_1065) from caulobacter crescentus CB15 at 1.87 a resolution

4GOQ · Hypothetical protein: “Crystal structure of a DUF1491 family protein (CC_1065) from caulobacter crescentus CB15 at 1.87 a resolution”. X-ray diffraction, 8 pockets (best druggability 0.70). MolNFT v1 #92973 on GenesisL1: 3D…

PDB: 4GOQ
Type: protein
Length: 531 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein
UniProt: Q9A9C4
Pockets: 8 · best druggability 0.70

Structure

x-ray diffraction · 4 distinct chains · 26% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein	protein	108	25% helix, 31% strand	Q9A9C4
B	Hypothetical protein	protein	105	27% helix, 30% strand	Q9A9C4
C	Hypothetical protein	protein	104	27% helix, 31% strand	Q9A9C4
D, E	Hypothetical protein	protein	107	26% helix, 32% strand	Q9A9C4

Ligands and binding sites

GOL · Glycerol · additive · 11 copies · chains A, B, C, D, E

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	784	0.70	0.76	53	empty
2	177	0.51	0.78	26	empty
3	102	0.46	0.79	14	empty
4	144	0.43	0.75	29	GOL
5	68	0.38	0.78	12	empty

Interfaces

8 interfaces between chains.

C–D · 610 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 608 Å² buried · 12 hydrogen bonds · protein-protein
A–E · 507 Å² buried · 6 hydrogen bonds · protein-protein
B–D · 427 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 379 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

4GOQ · Crystal structure of a DUF1491 family protein (CC_1065) from Caulobacter crescentus CB15… · 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 Q9A9C4
Elsewhere: RCSB PDB 4GOQ · PDBe 4GOQ · UniProt Q9A9C4

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