MolNFT v1 · #189577 · protein

Oxy-deoxy intermediate of V2 hemoglobin at 69% oxygen saturation

7VLD: “Oxy-deoxy intermediate of V2 hemoglobin at 69% oxygen saturation”. X-ray diffraction, 5 ligands (HEM, NAG, FUC). MolNFT v1 #189577 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7VLD
Type: protein
Length: 1,174 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: S0BBU7, S0BBR6, S0BCU7, S0BAP9
Ligands: HEM, NAG, FUC, CA, OXY

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	—	protein	146	—	S0BBU7
B, F	—	protein	144	—	S0BBR6
C, G	—	protein	149	—	S0BCU7
D, H	—	protein	148	—	S0BAP9

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 8 copies · chains A, D, B, C, E, H, F, G
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains D, H
FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A, D, E, H
CA · Calcium ion · metal · 2 copies · chains B, F
OXY · Oxygen molecule · ion · 8 copies · chains A, B, C, D, E, F, G, H

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

Compared structures

7VLD · Oxy-deoxy intermediate of V2 hemoglobin at 69% oxygen saturation · the same entry in another collection · chain D against D, 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 S0BBU7
Every structure of UniProt S0BBR6
Every structure of UniProt S0BCU7
Every structure of UniProt S0BAP9
Elsewhere: RCSB PDB 7VLD · PDBe 7VLD · UniProt S0BBU7 · UniProt S0BBR6 · UniProt S0BCU7 · UniProt S0BAP9

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