Structure of PDB 3edh Chain A

Receptor sequence
>3edhA (length=201) Species: 9606 (Homo sapiens) [Search protein sequence]
AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERT
DEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVG
FWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIM
HYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCP
A
3D structure
PDB3edh Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases
ChainA
Resolution1.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H92 E93 H96 H102 Y149
Catalytic site (residue number reindexed from 1) H93 E94 H97 H103 Y152
Enzyme Commision number 3.4.24.19: procollagen C-endopeptidase.
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 ZN A H92 H96 H102 H93 H97 H103
BS02 ZN A E103 Q189 E104 Q192
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:3edh, PDBe:3edh, PDBj:3edh
PDBsum3edh
PubMed
UniProtP13497|BMP1_HUMAN Bone morphogenetic protein 1 (Gene Name=BMP1)

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