1BP5: Protein

Human serum transferrin, recombinant N-terminal lobe, apo form. Determined by X-ray diffraction at 2.2 Å resolution. Released 13 Jan 1999.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,810
Mol. weight: 148.86 kDa
Released: 13 Jan 1999

Explore 1BP5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BP5 contains 78 α-helices and 64 β-strands across 4 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: 19 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	1
α-helix	13-27	15
β-strand	36-41	6	1
α-helix	45-53	9
β-strand	59	1	1
β-strand	60-62	3	2
α-helix	64-71	8
β-strand	77-84	8	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	116-119	4	4
α-helix	125-129	5
α-helix	130-135	6
α-helix	136-138	3
α-helix	140	1
α-helix	142	1
α-helix	146-153	8
β-strand	156-158	3	4
α-helix	168-171	4
α-helix	187-196	10
β-strand	202-206	5	4
α-helix	207-213	7
α-helix	217-220	4
β-strand	223-227	5	4
β-strand	231-233	3	4
α-helix	235-240	6
β-strand	244-247	4	4
β-strand	250-254	5	2
α-helix	260-274	15
β-strand	301-304	4	2
α-helix	305-306	2
α-helix	311-315	5
α-helix	317-328	12

Chain B: 19 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	5
α-helix	13-29	17
β-strand	36-41	6	5
α-helix	45-53	9
β-strand	59	1	5
β-strand	60-62	3	6
α-helix	64-71	8
β-strand	77-84	8	6
β-strand	85-86	2	7
β-strand	91-92	2	7
β-strand	94-102	9	8
α-helix	109-111	3
β-strand	117-119	3	8
α-helix	125-129	5
α-helix	130-135	6
α-helix	136-138	3
α-helix	140	1
α-helix	142	1
α-helix	146-153	8
β-strand	157-158	2	8
α-helix	168-171	4
α-helix	187-196	10
β-strand	202-206	5	8
α-helix	207-213	7
α-helix	217-220	4
β-strand	223-227	5	8
β-strand	231-233	3	8
α-helix	235-237	3
β-strand	244-247	4	8
β-strand	250-254	5	6
α-helix	260-274	15
β-strand	301-304	4	6
α-helix	305-306	2
α-helix	311-315	5
α-helix	317-328	12

Chain C: 20 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	9
α-helix	13-29	17
β-strand	36-41	6	9
α-helix	45-53	9
β-strand	59	1	9
β-strand	60-62	3	10
α-helix	64-71	8
β-strand	77-84	8	10
β-strand	85	1	11
β-strand	92	1	11
β-strand	94-102	9	12
α-helix	109-111	3
β-strand	116-119	4	12
α-helix	125-129	5
α-helix	130-135	6
α-helix	136-138	3
α-helix	140	1
α-helix	142	1
α-helix	146-151	6
β-strand	156-158	3	12
α-helix	168-171	4
α-helix	187-196	10
β-strand	202-206	5	12
α-helix	209-213	5
α-helix	217-220	4
β-strand	223-227	5	12
β-strand	231-234	4	12
α-helix	235-240	6
β-strand	244-247	4	12
β-strand	250-254	5	10
α-helix	260-274	15
β-strand	301-304	4	10
α-helix	305-306	2
α-helix	311-315	5
α-helix	317-328	12
α-helix	332-334	3

Chain D: 20 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	13
α-helix	13-29	17
β-strand	36-41	6	13
α-helix	45-53	9
β-strand	59	1	13
β-strand	60-62	3	14
α-helix	64-71	8
β-strand	77-84	8	14
β-strand	85	1	15
β-strand	92	1	15
β-strand	94-102	9	16
α-helix	109-111	3
β-strand	117-119	3	16
α-helix	125-129	5
α-helix	130-135	6
α-helix	136-138	3
α-helix	140	1
α-helix	142	1
α-helix	146-151	6
β-strand	157-158	2	16
α-helix	168-171	4
α-helix	187-196	10
β-strand	202-206	5	16
α-helix	209-213	5
α-helix	217-220	4
β-strand	223-226	4	16
β-strand	232-234	3	16
α-helix	235-240	6
β-strand	244-247	4	16
β-strand	250-254	5	14
α-helix	260-274	15
β-strand	301-304	4	14
α-helix	305-306	2
α-helix	311-315	5
α-helix	317-328	12
α-helix	332-334	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (serum transferrin)	A, B, C, D	protein	337	Homo sapiens	P02787 (AlphaFold model)

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

>1BP5_1 PROTEIN (SERUM TRANSFERRIN) (chains A, B, C, D)
VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAV
TLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHT
GLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCS
TLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKD
CHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAH
GFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTD

Primary citation

Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin. Jeffrey, P.D., Bewley, M.C., MacGillivray, R.T. et al. Biochemistry (1998) 37:13978-13986. DOI 10.1021/bi9812064 · 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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