Structure of PDB 1ciz Chain A

Receptor sequence

>1cizA (length=168) Species: 9606 (Homo sapiens)

FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPP

3D structure

• PDB: 1ciz X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity.
• Chain: A
• Resolution: 1.64 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H201 E202 H205 H211
• Catalytic site (residue number reindexed from 1): H119 E120 H123 H129
• Enzyme Commision number: 3.4.24.17: stromelysin 1.

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	ZN	A	H201 H205 H211	H119 H123 H129
BS02	ZN	A	H151 D153 H166 H179	H69 D71 H84 H97
BS03	CA	A	D158 G159 G161 V163 D181 E184	D76 G77 G79 V81 D99 E102
BS04	CA	A	D141 G173 N175 D177	D59 G91 N93 D95
BS05	CA	A	D107 D182 E184	D25 D100 E102
BS06	DPS	A	L164 A165 L197 H201 E202 H205 H211 P221 L222 Y223 H224 F232	L82 A83 L115 H119 E120 H123 H129 P139 L140 Y141 H142 F150	MOAD: Ki=36nM PDBbind-CN: -logKd/Ki=7.44,Ki=36nM

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:1ciz, PDBe:1ciz, PDBj:1ciz
• PDBsum: 1ciz
• PubMed: 10422833
• UniProt: P08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)