Structure of PDB 2clt Chain B

Receptor sequence

>2cltB (length=367) Species: 9606 (Homo sapiens)

FVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTF
TKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDE
DERWTNNFREYNLHRVAAHALGHSLGLSHSTDIGALMYPSYTFSGDVQLA
QDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKD
RFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYW
AVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWR
YDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDP
KTKRILTLQKANSWFNC

3D structure

• PDB: 2clt Crystal Structure of an Active Form of Human Mmp-1.
• Chain: B
• Resolution: 2.67 Å

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.

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	CA	B	D105 E180 E182	D25 E100 E102
BS02	CA	B	D266 E310 D359 D408	D186 E230 D279 D328
BS03	CA	B	D139 G171 I172 G173 D175	D59 G91 I92 G93 D95
BS04	CA	B	D156 G157 G159 N161 D179 E182	D76 G77 G79 N81 D99 E102
BS05	ZN	B	H149 D151 H164 H177	H69 D71 H84 H97
BS06	ZN	B	H199 H203 H209	H119 H123 H129

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)