MolNFT v1 · #161273 · protein

Crystal structure of human GDP-D-mannose 4,6-dehydratase (S156D) in complex with GDP-man

6Q94: “Crystal structure of human GDP-D-mannose 4,6-dehydratase (S156D) in complex with GDP-man”. X-ray diffraction, 2 ligands (NAP, GDD). MolNFT v1 #161273 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6Q94
Type: protein
Length: 2,776 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O60547
Ligands: NAP, GDD

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	—	protein	344	—	O60547
A, E, F, G	—	protein	350	—	O60547
C	—	protein	348	—	O60547
D	—	protein	343	—	O60547
H	—	protein	341	—	O60547

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 8 copies · chains B, A, C, E, D, F, G, H
GDD · Guanosine-5'-diphosphate-alpha-D-mannose · ligand · 8 copies · chains B, A, C, D, E, F, G, H
EDO · 1,2-ethanediol · additive · 4 copies · chains D, F, G, H

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

Compared structures

6Q94 · Crystal structure of human GDP-D-mannose 4,6-dehydratase (S156D) in complex with GDP-Man · the same entry in another collection · chain H against H, TM-score 1.00
O60547 · AlphaFold monomer V2.0 prediction for GDP-mannose 4,6 dehydratase (O60547) · a predicted model of the same protein · chain B 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 O60547
Elsewhere: RCSB PDB 6Q94 · PDBe 6Q94 · UniProt O60547

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