BioLiP

Receptor Information

>1umt Chain A (length=166) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGP

Ligand ID

0DS

InChI

InChI=1S/C23H36N4O5/c1-14(2)10-17(13-20(28)27-32)22(30)26-19(11-15(3)4)23(31)25-18(21(24)29)12-16-8-6-5-7-9-16/h5-9,14-15,17-19,32H,10-13H2,1-4H3,(H2,24,29)(H,25,31)(H,26,30)(H,27,28)/t17-,18+,19+/m1/s1

InChIKey

HLSQLCOADIMQBK-QYZOEREBSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N
ACDLabs 10.04	O=C(NO)CC(C(=O)NC(C(=O)NC(C(=O)N)Cc1ccccc1)CC(C)C)CC(C)C
OpenEye OEToolkits 1.5.0	CC(C)CC(CC(=O)NO)C(=O)NC(CC(C)C)C(=O)NC(Cc1ccccc1)C(=O)N
CACTVS 3.341	CC(C)C[CH](CC(=O)NO)C(=O)N[CH](CC(C)C)C(=O)N[CH](Cc1ccccc1)C(N)=O
CACTVS 3.341	CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(N)=O

Formula

C23 H36 N4 O5

Name

N-{(2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-L-leucyl-L-phenylalaninamide;
ICI U24522

PDB chain

1umt Chain A Residue 261 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	1umt Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor.
Resolution	N/A
Binding residue (original residue number in PDB)	Y155 N162 V163 T191 L197 H201 H211 Y220 P221 L222
Binding residue (residue number reindexed from 1)	Y73 N80 V81 T109 L115 H119 H129 Y138 P139 L140
Annotation score	1
Binding affinity	BindingDB: Ki=127nM

Catalytic site (original residue number in PDB)	H201 E202 H205 H211
Catalytic site (residue number reindexed from 1)	H119 E120 H123 H129
Enzyme Commision number	3.4.24.17: stromelysin 1.

	Molecular Function
GO:0004222	metalloendopeptidase activity
GO:0008237	metallopeptidase activity
GO:0008270	zinc ion binding

	Biological Process
GO:0006508	proteolysis

	Cellular Component
GO:0031012	extracellular matrix

PDB	RCSB:1umt, PDBe:1umt, PDBj:1umt
PDBsum	1umt
PubMed	8580839
UniProt	P08254\|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

[Back to BioLiP]

Structure of PDB 1umt Chain A Binding Site BS04