Structure of PDB 5amm Chain A

Receptor sequence
>5ammA (length=267) Species: 5664 (Leishmania major) [Search protein sequence]
SEEPPFDIRALRADIEDMISEKLELGPSLIRLAWHEAASYDCFKKDGSPN
SASMRFKPECLYAGNKGLDIPRKALETLKKKYPQISYADLWVLAAYVAIE
YMGGPTIPFCWGRVDAKDGSVCGPDGRLPDGSKTQSHVREVFRRLGFNDQ
ETVALIGAHTCGECHIEFSGYHGPWTHNKNGFDNSFFTQLLDEDWVLNPK
VEQMQLMDRATTKLMMLPSDVCLLLDPSYRKYVELYAKDNDRFNKDFANA
FKKLTELGTRNLHKAPA
3D structure
PDB5amm Bind and Crawl" Association Mechanism of Leishmania Major Peroxidase and Cytochrome C Revealed by Brownian and Molecular Dynamics Simulations.
ChainA
Resolution2.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R64 H68 H192 W208 D253
Catalytic site (residue number reindexed from 1) R31 H35 H159 W175 D220
Enzyme Commision number 1.11.1.5: cytochrome-c peroxidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A P60 R64 W67 P162 G164 L188 A191 H192 G195 E196 C197 H198 F201 S202 W208 F284 P27 R31 W34 P129 G131 L155 A158 H159 G162 E163 C164 H165 F168 S169 W175 F251
BS02 CA A E69 S72 S81 S86 E92 E36 S39 S48 S53 E59
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
Biological Process
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress

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Molecular Function
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Biological Process
External links
PDB RCSB:5amm, PDBe:5amm, PDBj:5amm
PDBsum5amm
PubMed26598276
UniProtQ4Q3K2

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