Structure of PDB 2clt Chain B Binding Site BS01

Receptor Information

>2clt Chain B (length=367) Species: 9606 (Homo sapiens)

FVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTF
TKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDE
DERWTNNFREYNLHRVAAHALGHSLGLSHSTDIGALMYPSYTFSGDVQLA
QDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKD
RFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYW
AVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWR
YDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDP
KTKRILTLQKANSWFNC

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 2clt Chain B Residue 1301

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2clt Crystal Structure of an Active Form of Human Mmp-1.
• Resolution: 2.67 Å
• Binding residue (original residue number in PDB): D105 E180 E182
• Binding residue (residue number reindexed from 1): D25 E100 E102
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): H199 A200 H203 H209
• Catalytic site (residue number reindexed from 1): H119 A120 H123 H129
• Enzyme Commision number: 3.4.24.7: interstitial 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

External links

• PDB: RCSB:2clt, PDBe:2clt, PDBj:2clt
• PDBsum: 2clt
• PubMed: 16890240
• UniProt: P03956|MMP1_HUMAN Interstitial collagenase (Gene Name=MMP1)