Structure of PDB 1su3 Chain A Binding Site BS04

Receptor Information
>1su3 Chain A (length=415) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLVQKYLEKYYNLKGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCG
VPDVAPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTK
VSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDE
RWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQD
DIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRF
YMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAV
QGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYD
EYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKT
KRILTLQKANSWFNC
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1su3 Chain A Residue 904 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1su3 X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D285 E329 D378 D427
Binding residue
(residue number reindexed from 1)		D234 E278 D327 D376
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H167 E168 H171 H177
Enzyme Commision number 3.4.24.7: interstitial collagenase.
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0022617 extracellular matrix disassembly
GO:0030198 extracellular matrix organization
GO:0030574 collagen catabolic process
GO:0031334 positive regulation of protein-containing complex assembly
GO:0071492 cellular response to UV-A
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0031012 extracellular matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1su3, PDBe:1su3, PDBj:1su3
PDBsum1su3
PubMed15611040
UniProtP03956|MMP1_HUMAN Interstitial collagenase (Gene Name=MMP1)

[Back to BioLiP]