Structure of PDB 1fbl Chain A

Receptor sequence

>1fblA (length=367) Species: 9823 (Sus scrofa)

FVLTPGNPRWENTHLTYRIENYTPDLSREDVDRAIEKAFQLWSNVSPLTF
TKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDE
DERWTKNFRDYNLYRVAAHELGHSLGLSHSTDIGALMYPNYIYTGDVQLS
QDDIDGIQAIYGPSENPVQPSGPQTPQVCDSKLTFDAITTLRGELMFFKD
RFYMRTNSFYPEVELNFISVFWPQVPNGLQAAYEIADRDEVRFFKGNKYW
AVRGQDVLYGYPKDIHRSFGFPSTVKNIDAAVFEEDTGKTYFFVAHECWR
YDEYKQSMDTGYPKMIAEEFPGIGNKVDAVFQKDGFLYFFHGTRQYQFDF
KTKRILTLQKANSWFNC

3D structure

• PDB: 1fbl Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H119 E120 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	A	D124 E199 E201	D25 E100 E102
BS02	CA	A	D285 Q329 D378 D427	D186 Q230 D279 D328
BS03	CA	A	D158 G190 G192 D194	D59 G91 G93 D95
BS04	CA	A	D175 G176 G178 N180 D198 E201	D76 G77 G79 N81 D99 E102
BS05	ZN	A	H168 D170 H183 H196	H69 D71 H84 H97
BS06	ZN	A	H218 H222 H228	H119 H123 H129
BS07	HTA	A	G179 N180 L181 A182 H218 E219 H222 H228 P238 N239 Y240	G80 N81 L82 A83 H119 E120 H123 H129 P139 N140 Y141

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:1fbl, PDBe:1fbl, PDBj:1fbl
• PDBsum: 1fbl
• PubMed: 8590015
• UniProt: P21692|MMP1_PIG Interstitial collagenase (Gene Name=MMP1)