1nwr Summary


Crystal structure of human cartilage gp39 (HC-gp39)

The structure was published by Fusetti, F., Pijning, T., Kalk, K.H., Bos, E., and Dijkstra, B.W., in 2003 in a paper entitled "Crystal Structure and Carbohydrate-binding Properties of the Human Cartilage Glycoprotein-39" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2003.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Chitinase-3 like protein 1.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Chitinase-3 like protein 1 P36222 (22-383) (CH3L1_HUMAN)search Homo sapienssearch 100% 362 100%
B Chitinase-3 like protein 1 P36222 (22-383) (CH3L1_HUMAN)search Homo sapienssearch 100% 362 100%
C Chitinase-3 like protein 1 P36222 (22-383) (CH3L1_HUMAN)search Homo sapienssearch 100% 362 100%
D Chitinase-3 like protein 1 P36222 (22-383) (CH3L1_HUMAN)search Homo sapienssearch 100% 362 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P36222 (22 - 383) Chitinase-3 like protein 1 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P36222) Type II chitinasesearch, Chitinase insertion domainsearch Glycosidasessearch, Chitinase A; domain 3search PF00704: Glycosyl hydrolases family 18search

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A, B, C, D (P36222) extracellular spacesearch extracellular regionsearch endoplasmic reticulumsearch perinuclear region of cytoplasmsearch extracellular vesicular exosomesearch cytoplasmsearch proteinaceous extracellular matrixsearch positive regulation of peptidyl-threonine phosphorylationsearch inflammatory responsesearch response to interleukin-6search lung developmentsearch interleukin-8 secretionsearch cellular response to tumor necrosis factorsearch apoptotic processsearch activation of NF-kappaB-inducing kinase activitysearch positive regulation of ERK1 and ERK2 cascadesearch response to tumor necrosis factorsearch response to mechanical stimulussearch positive regulation of protein kinase B signalingsearch response to interleukin-1search cartilage developmentsearch positive regulation of angiogenesissearch chitin catabolic processsearch carbohydrate metabolic processsearch immune responsesearch carbohydrate bindingsearch chitinase activitysearch chitin bindingsearch extracellular matrix structural constituentsearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch

Chain InterPro annotation
A, B, C, D Glycoside hydrolase, family 18, catalytic domainsearch Chitinase IIsearch Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch Chitinase-3-like protein 1search Chitinase insertion domainsearch