PDBsum entry 5e83

Oxygen transport

PDB id: 5e83

Contents

Protein chains

141 a.a.

146 a.a.

Ligands

HEM-CMO ×4

5L7

GOL ×3

UNL

Waters ×400

PDB id:

5e83

Name:

Oxygen transport

Title:

Crystal structure of carbonmonoxy hemoglobin s (liganded sickle cell hemoglobin) complexed with gbt440, co-crystallization experiment

Structure:

Hemoglobin subunit alpha. Chain: a, c. Synonym: alpha-globin,hemoglobin alpha chain. Hemoglobin subunit beta. Chain: b, d. Synonym: beta-globin,hemoglobin beta chain

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606

Resolution:

1.80Å R-factor: 0.178 R-free: 0.208

Authors:

L.Patskovska,Y.Patskovsky,J.B.Bonanno,S.C.Almo

Key ref:

D.Oksenberg et al. (2016). GBT440 increases haemoglobin oxygen affinity, reduces sickling and prolongs RBC half-life in a murine model of sickle cell disease. Br J Haematol, 175, 141-153. PubMed id: 27378309 DOI: 10.1111/bjh.14214

Date:

13-Oct-15 Release date: 20-Jul-16

Protein chains

P69905  (HBA_HUMAN) -  Hemoglobin subunit alpha from Homo sapiens

Seq: 142 a.a.

Struc: 141 a.a.

Protein chains

P68871  (HBB_HUMAN) -  Hemoglobin subunit beta from Homo sapiens

Seq: 147 a.a.

Struc: 146 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1111/bjh.14214

Br J Haematol 175:141-153 (2016)

PubMed id: 27378309

GBT440 increases haemoglobin oxygen affinity, reduces sickling and prolongs RBC half-life in a murine model of sickle cell disease.

D.Oksenberg, K.Dufu, M.P.Patel, C.Chuang, Z.Li, Q.Xu, A.Silva-Garcia, C.Zhou, A.Hutchaleelaha, L.Patskovska, Y.Patskovsky, S.C.Almo, U.Sinha, B.W.Metcalf, D.R.Archer.

ABSTRACT

No abstract given.