2CLT: Interstitial collagenase

Crystal structure of the active form (full-length) of human fibroblast collagenase. Determined by X-ray diffraction at 2.67 Å resolution. Released 9 Aug 2006.

Method
X-ray diffraction
Resolution
2.67 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
6,007
Mol. weight
85.04 kDa
Ligands
ZN, CA
Released
9 Aug 2006

Explore 2CLT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CLT contains 24 α-helices and 54 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 27 β-strands

ElementResiduesLengthSheet
β-strand8311
α-helix841
β-strand94-9962
α-helix108-12316
β-strand129-13242
β-strand140-14562
β-strand163-16532
α-helix166-1672
β-strand176-17942
β-strand18513
β-strand19213
α-helix193-20513
β-strand20711
α-helix231-24111
α-helix253-2564
β-strand267-27154
β-strand274-27964
β-strand282-28654
β-strand294-29744
α-helix298-3003
α-helix3061
β-strand311-31555
β-strand320-32565
β-strand328-33365
β-strand336-33725
α-helix3381
β-strand34415
α-helix345-3495
β-strand360-36346
β-strand369-37466
β-strand377-38266
α-helix383-3853
β-strand387-38826
β-strand394-39526
α-helix396-3994
β-strand409-41357
β-strand416-42167
β-strand424-42967
β-strand434-44077
Chain B: 12 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand8318
α-helix841
β-strand94-9969
α-helix108-12316
β-strand129-13249
β-strand140-14569
β-strand163-16539
α-helix166-1672
β-strand176-17949
β-strand185110
β-strand192110
α-helix193-20412
β-strand20718
α-helix231-24111
α-helix253-2564
β-strand267-271511
β-strand274-279611
β-strand282-286511
β-strand294-297411
α-helix298-3014
α-helix305-3062
β-strand311-315512
α-helix316-3183
β-strand320-325612
β-strand328-333612
β-strand336-337212
β-strand343-344212
α-helix345-3484
β-strand360-363413
β-strand369-374613
β-strand377-382613
β-strand387-388213
β-strand394-395213
α-helix396-3994
β-strand409-412414
β-strand417-421514
β-strand424-428514
β-strand437-440414
α-helix441-4444

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interstitial collagenaseA, Bprotein367HOMO SAPIENSP03956 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2CLT_1 INTERSTITIAL COLLAGENASE (chains A, B)
FVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADI
MISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHA
LGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACD
SKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDE
VRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWR
YDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQK
ANSWFNC

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4
CACalcium ionCa8

Primary citation

Crystal Structure of an Active Form of Human Mmp-1. Iyer, S., Visse, R., Nagase, H. et al. J Mol Biol (2006) 362:78. DOI 10.1016/J.JMB.2006.06.079 · PubMed

Other PDB entries of the same protein (UniProt P03956 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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