2DOI: Angiostatin

The X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound to a peptide from the group A streptococcus protein PAM. Determined by X-ray diffraction at 3.1 Å resolution. Released 5 Dec 2006.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,064
Mol. weight: 60.79 kDa
Released: 5 Dec 2006

Explore 2DOI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2DOI contains 10 α-helices and 40 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: 3 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	85	1	11
α-helix	104	1
β-strand	105	1	12
α-helix	106-107	2
β-strand	134	1	13
β-strand	144-146	3	13
β-strand	147	1	12
β-strand	154-156	3	13
α-helix	160	1
β-strand	161	1	11
β-strand	167	1	14
β-strand	180	1	15
β-strand	181	1	16
β-strand	186	1	15
β-strand	187	1	17
β-strand	216	1	18
β-strand	225-227	3	18
β-strand	228	1	17
β-strand	235-237	3	18
β-strand	238	1	16
β-strand	242	1	14

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	306-325	20

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	308-325	18

Chain X: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	85	1	1
β-strand	98	1	2
β-strand	99	1	3
β-strand	104	1	2
β-strand	105	1	4
α-helix	106-107	2
β-strand	134	1	5
β-strand	144-146	3	5
β-strand	147	1	4
β-strand	154-156	3	5
β-strand	157	1	3
β-strand	161	1	1
β-strand	167	1	6
β-strand	180	1	7
β-strand	181	1	8
α-helix	185	1
β-strand	186	1	7
β-strand	187	1	9
α-helix	188-189	2
α-helix	206-208	3
β-strand	216	1	10
β-strand	225-227	3	10
β-strand	228	1	9
β-strand	235-237	3	10
β-strand	238	1	8
α-helix	240-241	2
β-strand	242	1	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiostatin	A, X	protein	234	Homo sapiens	P00747 (AlphaFold model)
Plasminogen-binding group A streptococcal M-like protein PAM	B, C	protein	30		P49054 (AlphaFold model)

Sequence of entity 1 (A, X), FASTA

>2DOI_1 Angiostatin (chains A, X)
LSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDP
QGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGY
IPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGT
GENYRGNVAVTVSGHTCQHWSAQTPHTHERTPENFPCKNLDENYCRNPDGKRAP

Sequence of entity 2 (B, C), FASTA

>2DOI_2 Plasminogen-binding group A streptococcal M-like protein PAM (chains B, C)
VEKLTADAELQRLKNERHEEAELERLKSEY

Primary citation

X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound to a peptide from the group A streptococcal surface protein PAM. Cnudde, S.E., Prorok, M., Castellino, F.J. et al. Biochemistry (2006) 45:11052-11060. DOI 10.1021/bi060914j · PubMed

Other PDB entries of the same protein (UniProt P00747 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5UGG 1.2 Å, Protease Inhibitor
6D3Y 1.32 Å, Highly Potent and Selective Plasmin Inhibitors Based on the Sunflower Trypsin…
5UGD 1.38 Å, Protease Inhibitor
6D40 1.43 Å, Highly Potent and Selective Plasmin Inhibitors Based on the Sunflower Trypsin…
8F7U 1.47 Å, Macrocyclic Plasmin Inhibitor
7UAH 1.57 Å, Macrocyclic plasmin inhibitor
8F7V 1.65 Å, Macrocyclic plasmin inhibitor
5HPG 1.66 Å, Structure and ligand determinants of the recombinant kringle 5 domain of human plasminogen
1KRN 1.67 Å, Structure of kringle 4 at 4C temperature and 1.67 Å resolution
6OG4 1.7 Å, plasminogen binding group A streptococcal M protein
1KI0 1.75 Å, The X-ray Structure of Human Angiostatin
4CIK 1.78 Å, plasminogen kringle 1 in complex with inhibitor

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