Brand  (β version)

PDB ID: 3AYK

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Ligands
Code Name Style Show Link
CA Calcium ion PoSSuM
CGS N-hydroxy-2(R)-[[(4-methoxyphenyl)sulfonyl](3-picolyl)amino]-3-methylbutanamide hydrochloride PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Structure summary

Code : 3AYK   PDBj   RCSB PDB   PDBe
Header : MATRIX METALLOPROTEINASE
Title : CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, MINIMIZED AVERAGE STRUCTURE
Release Data : 1999-06-07
Compound :
mol_id molecule chains synonym
1 PROTEIN (COLLAGENASE) A MMP-1, FIBROBLAST COLLAGENASE
ec: 3.4.24.7
fragment: CATALYTIC FRAGMENT
other_details: HETEROGEN: N-HYDROXY-2(R)-[[(4-METHOXYPHENYL) SULFONYL](3-PICOLYL)AMINO]-3- METHYLBUTANAMIDE HYDROCHLORIDE
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
strain: BL21 (DE3)
expression_system_strain: BL21 (DE3)
expression_system_vector: PET-21A(+)
expression_system_plasmid: PNOT-3A
Authors : Powers, R., Moy, F.J.
Keywords : MATRIX METALLOPROTEINASE, HYDROLASE, METALLOPROTEASE, GLYCOPROTEIN
Exp. method : SOLUTION NMR
Citation :

NMR solution structure of the catalytic fragment of human fibroblast collagenase complexed with a sulfonamide derivative of a hydroxamic acid compound.

Moy, F.J.,Chanda, P.K.,Chen, J.M.  et al.
(1999)  Biochemistry  38 : 7085 - 7096

PubMed: 10353819
DOI: 10.1021/bi982576v

High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.

Moy, F.J.,Chanda, P.K.,Cosmi, S.  et al.
(1998)  Biochemistry  37 : 1495 - 1504

PubMed: 9484219
DOI: 10.1021/bi972181w

Assignments, secondary structure and dynamics of the inhibitor-free catalytic fragment of human fibroblast collagenase.

Moy, F.J.,Pisano, M.R.,Chanda, P.K.  et al.
(1997)  J.Biomol.Nmr  10 : 9 - 19

PubMed: 9335112
DOI: 10.1023/a:1018362914316

Reaction

Chain : A
UniProt : P03956 (MMP1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Cleavage of the triple helix of collagen at about three- quarters of the length of the molecule from the N-terminus, at 775- Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue. 3.4.24.7 PubMed:1645757, PubMed:16807369, PubMed:2153297, PubMed:2557822
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