Structure of PDB 1a85 Chain A Binding Site BS05

Receptor Information
>1a85 Chain A (length=158) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQG
EADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTN
TSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDI
DGIQAIYG
Ligand information
Ligand ID0DY
InChIInChI=1S/C18H27N5O5/c1-10(2)6-13(17(26)23-28)16(25)22-14(8-15(20)24)18(27)21-9-11-4-3-5-12(19)7-11/h3-5,7,10,13-14,28H,6,8-9,19H2,1-2H3,(H2,20,24)(H,21,27)(H,22,25)(H,23,26)/t13-,14-/m0/s1
InChIKeyLYVDOPZAZLWTSE-KBPBESRZSA-N
SMILES
SoftwareSMILES
CACTVS 3.352CC(C)C[C@@H](C(=O)NO)C(=O)N[C@H](CC(N)=O)C(=O)NCc1cccc(N)c1
CACTVS 3.352CC(C)C[CH](C(=O)NO)C(=O)N[CH](CC(N)=O)C(=O)NCc1cccc(N)c1
ACDLabs 10.04O=C(NO)C(C(=O)NC(C(=O)NCc1cc(N)ccc1)CC(=O)N)CC(C)C
FormulaC18 H27 N5 O5
NameN~1~-(3-aminobenzyl)-N~2~-[(2R)-2-(hydroxycarbamoyl)-4-methylpentanoyl]-L-aspartamide;
HONH-iBM-Asn-NHBn(m-NH2)
ChEMBL
DrugBank
ZINCZINC000013528382
PDB chain1a85 Chain A Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1a85 Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		I159 L160 A161 L193 H197 E198 H201 H207 L214 Y216 N218 Y219
Binding residue
(residue number reindexed from 1)		I75 L76 A77 L109 H113 E114 H117 H123 L130 Y132 N134 Y135
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=4.52,IC50=30uM
BindingDB: Ki=26000nM
Enzymatic activity
Catalytic site (original residue number in PDB) H197 E198 H201 H207
Catalytic site (residue number reindexed from 1) H113 E114 H117 H123
Enzyme Commision number 3.4.24.34: neutrophil collagenase.
Gene Ontology
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1a85, PDBe:1a85, PDBj:1a85
PDBsum1a85
PubMed9655333
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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