1OQH: R124A mutant of the N-lobe human transferrin

Crystal Structure of the R124A mutant of the N-lobe human transferrin. Determined by X-ray diffraction at 2.4 Å resolution. Released 18 Mar 2003.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,687
Mol. weight: 37.28 kDa
Ligands: CO3, FE
Released: 18 Mar 2003

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

Secondary structure: helices and β-sheets

1OQH contains 20 α-helices and 16 β-strands across 1 chain. 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: 20 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	1
α-helix	13-29	17
β-strand	36-42	7	1
α-helix	45-54	10
β-strand	59	1	1
β-strand	60-62	3	2
α-helix	64-71	8
β-strand	78-84	7	2
β-strand	85-86	2	3
β-strand	91-92	2	3
β-strand	94-102	9	4
α-helix	109-111	3
β-strand	117-119	3	4
α-helix	125-129	5
α-helix	130-134	5
α-helix	136-138	3
α-helix	140	1
α-helix	142	1
α-helix	146-153	8
β-strand	157-158	2	4
α-helix	168-170	3
α-helix	188-196	9
β-strand	202-206	5	4
α-helix	209-213	5
α-helix	217-220	4
β-strand	223-226	4	4
β-strand	232-234	3	4
α-helix	235-240	6
β-strand	244-247	4	4
α-helix	248-249	2
β-strand	250-253	4	2
α-helix	260-273	14
β-strand	301-304	4	2
α-helix	305-306	2
α-helix	311-315	5
α-helix	317-327	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serotransferrin	A	protein	337	Homo sapiens	P02787 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1OQH_1 Serotransferrin (chains A)
VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAV
TLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHT
GLGASAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCS
TLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKD
CHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAH
GFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPDT

Ligands and cofactors

ID	Name	Formula	Copies
CO3	Carbonate ion	C O3	1
FE	FE (III) ion	Fe	1

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

Primary citation

Structural and functional consequences of binding site mutations in transferrin: crystal structures of the Asp63Glu and Arg124Ala mutants of the N-lobe of human transferrin. Baker, H.M., He, Q.-Y., Briggs, S.K. et al. Biochemistry (2003) 42:7084-7089. DOI 10.1021/bi020689f · PubMed

Other PDB entries of the same protein (UniProt P02787 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1RYO 1.2 Å, Human serum transferrin, N-lobe bound with oxalate
1A8E 1.6 Å, Human serum transferrin, recombinant N-terminal lobe
3SKP 1.7 Å, The structure of apo-human transferrin C-lobe with bound sulfate ions
1A8F 1.8 Å, Human serum transferrin, recombinant N-terminal lobe
1D3K 1.8 Å, Human serum transferrin
1FQE 1.8 Å, Crystal structures of mutant (K206A) that abolish the dilysine interaction in the N-lobe…
3FGS 1.8 Å, Crystal structure of G65R/K206E double mutant of the N-lobe human transferrin
1JQF 1.85 Å, Human Transferrin N-Lobe Mutant H249Q
1OQG 1.9 Å, Crystal structure of the D63E mutant of the N-lobe human transferrin
9RTB 1.93 Å, Crystal structure of the adduct formed upon reaction of [V(IV)O(acetylacetonate)2] with…
1D4N 2.0 Å, Human serum transferrin
1N84 2.05 Å, Human serum transferrin, N-lobe

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