1BHQ: Mac-1 I domain cadmium complex

Mac-1 I domain cadmium complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 4 Nov 1998.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,200
Mol. weight: 43.75 kDa
Ligands: ACE, CD
Released: 4 Nov 1998

Explore 1BHQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BHQ contains 27 α-helices and 14 β-strands across 2 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 1: 13 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	134-140	7	1
α-helix	147-163	17
β-strand	170-176	7	1
β-strand	180-184	5	1
α-helix	186-189	4
α-helix	195-199	5
α-helix	211-217	7
α-helix	218-222	5
α-helix	225-227	3
β-strand	235-241	7	1
α-helix	256-261	6
β-strand	264-271	8	1
α-helix	273-275	3
α-helix	281-287	7
α-helix	289	1
α-helix	292-295	4
β-strand	296-299	4	1
α-helix	305-308	4
α-helix	309-315	7

Chain 2: 14 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	434-440	7	2
β-strand	442	1	3
α-helix	449-464	16
β-strand	470-476	7	2
β-strand	480-484	5	2
α-helix	486-489	4
α-helix	495-499	5
β-strand	506	1	3
α-helix	511-517	7
α-helix	518-522	5
α-helix	525-527	3
β-strand	535-541	7	2
α-helix	552-562	11
β-strand	564-571	8	2
α-helix	573-576	4
α-helix	580-587	8
α-helix	589	1
α-helix	591	1
α-helix	592-594	3
β-strand	596-599	4	2
α-helix	603-608	6
α-helix	609-618	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CD11B	1, 2	protein	189	Homo sapiens	P11215 (AlphaFold model)

Sequence of entity 1 (1, 2), FASTA

>1BHQ_1 CD11B (chains 1, 2)
SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIHFTFKEFQNN
PNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGY
EDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVNNFEALKTIQNQL
REKIFAIEG

Ligands and cofactors

ID	Name	Formula	Copies
ACE	Acetyl group	C2 H4 O	2
CD	Cadmium ion	Cd	3

Primary citation

Cation binding to the integrin CD11b I domain and activation model assessment. Baldwin, E.T., Sarver, R.W., Bryant Jr., G.L. et al. Structure (1998) 6:923-935. DOI 10.1016/S0969-2126(98)00093-8 · PubMed

Other PDB entries of the same protein (UniProt P11215 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1MF7 1.25 Å, Integrin alpha M I domain
1NA5 1.5 Å, Integrin alpha M I domain
8CE6 1.58 Å, Crystal structure of human Cd11b I domain in P212121 space group
1IDO 1.7 Å, I-domain from integrin CR3, MG2+ bound
1JLM 2.0 Å, I-domain from integrin CR3, MN2+ bound
4XW2 2.0 Å, Structural basis for simvastatin competitive antagonism of complement receptor 3
8CE9 2.11 Å, Crystal structure of human Cd11b I domain in C121 space group
1M1U 2.3 Å, An isoleucine-based allosteric switch controls affinity and shape shifting in integrin…
1N9Z 2.5 Å, Integrin alpha M I domain mutant
9RM9 2.6 Å, Cryo-EM structure of alphaM/beta2 headpiece complex without alphaM I-domain - the…
1BHO 2.7 Å, Mac-1 I domain magnesium complex
1IDN 2.7 Å, Mac-1 I domain metal free

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