8HPZ: PDB entry 8HPZ

Crystal structure of the MlaD domain of the MlaD protein from Escherichia coli (Form I). Determined by X-ray diffraction at 2.3 Å resolution. Released 10 Jan 2024.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Escherichia coli K-12
Chains: 3
Atoms: 2,488
Mol. weight: 52.49 kDa
Ligands: CO2
Released: 10 Jan 2024

Explore 8HPZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8HPZ contains 5 α-helices and 30 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	1
β-strand	57-60	4	1
β-strand	63-73	11	1
β-strand	80-87	8	1
β-strand	94	1	2
β-strand	98-103	6	1
β-strand	110-115	6	1
α-helix	116-118	3
α-helix	121-123	3
β-strand	127	1	2
β-strand	132-133	2	1
β-strand	136-138	3	1

Chain B: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	3
β-strand	57-60	4	3
β-strand	63-73	11	3
β-strand	80-87	8	3
β-strand	94	1	4
β-strand	98-103	6	3
β-strand	110-115	6	3
α-helix	116-118	3
α-helix	121-123	3
β-strand	127	1	4
β-strand	133	1	3
β-strand	136-138	3	3

Chain C: 1 helix, 10 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	5
β-strand	57-60	4	5
β-strand	63-73	11	5
β-strand	80-87	8	5
β-strand	94	1	6
β-strand	98-103	6	5
β-strand	110-115	6	5
α-helix	121-123	3
β-strand	127	1	6
β-strand	132-133	2	5
β-strand	136-138	3	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Intermembrane phospholipid transport system binding protein MlaD	A, B, C	protein	162	Escherichia coli K-12	P64604 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>8HPZ_1 Intermembrane phospholipid transport system binding protein MlaD (chains A, B, C)
MHHHHHHANVTSIRTEPTYTLYATFDNIGGLKARSPVSIGGVVVGRVADITLDPKTYLPR
VTLEIEQRYNHIPDTSSLSIRTSGLLGEQYLALNVGFEDPELGTAILKDGDTIQDTKSAM
VLEDLIGQFLYGSKGDDNKNSGDAPAAAPGNNETTEPVGTTK

Ligands and cofactors

ID	Name	Formula	Copies
CO2	Carbon dioxide	C O2	1

Water and common crystallization additives (EDO) are not listed.

Primary citation

The Structural Features of MlaD Illuminate its Unique Ligand-Transporting Mechanism and Ancestry. Dutta, A., Kanaujia, S.P. Protein J (2024) 43:298-315. DOI 10.1007/s10930-023-10179-5 · PubMed

Other PDB entries of the same protein (UniProt P64604 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8HQ9 2.7 Å, Crystal structure of the MlaD domain of the MlaD protein from Escherichia coli (Form II)
7CGE 2.9 Å, The overall structure of nucleotide free MlaFEDB complex
6XBD 3.05 Å, Cryo-EM structure of MlaFEDB in nanodiscs with phospholipid substrates
8HQA 3.2 Å, Crystal structure of the ectodomain of the MlaD protein from Escherichia coli in the…
6ZY3 3.3 Å, Cryo-EM structure of MlaFEDB in complex with phospholipid
6ZY9 3.3 Å, Cryo-EM structure of MlaFEDB in complex with AMP-PNP
6ZY2 3.6 Å, Cryo-EM structure of apo MlaFEDB
7CH0 3.7 Å, The overall structure of the MlaFEDB complex in ATP-bound EQclose conformation (Mutation…
6ZY4 4.1 Å, Cryo-EM structure of MlaFEDB in complex with ADP
7CGN 4.3 Å, The overall structure of the MlaFEDB complex in ATP-bound EQtall conformation (Mutation…
8OJ4 4.35 Å, Structure of the MlaCD complex (1:6 stoichiometry)
8OJG 4.38 Å, Structure of the MlaCD complex (2:6 stoichiometry)

Browse structure collections

About this viewer

MolViewer shows 8HPZ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.