4P3C: MT1-MMP:Fab complex

MT1-MMP:Fab complex (Form I). Determined by X-ray diffraction at 1.94 Å resolution. Released 17 Dec 2014.

Method
X-ray diffraction
Resolution
1.94 Å
Organisms
Mus musculus, Homo sapiens
Chains
3
Atoms
3,992
Mol. weight
49.87 kDa
Ligands
MG
Released
17 Dec 2014

Explore 4P3C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4P3C contains 16 α-helices and 48 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 H: 10 helices, 23 β-strands

ElementResiduesLengthSheet
β-strand3-751
β-strand11-1222
β-strand18-2581
α-helix29-313
β-strand34-3963
β-strand45-5173
β-strand58-6033
α-helix62-643
β-strand68-7361
α-helix74-763
β-strand78-8361
α-helix88-903
β-strand92-10093
β-strand103-10863
β-strand112-11433
β-strand115-11622
α-helix120-1212
β-strand12214
α-helix123-1242
β-strand125-12955
β-strand140-150115
β-strand15114
β-strand156-15946
α-helix160-1623
β-strand16416
β-strand168-17035
α-helix171-1733
β-strand174-17635
β-strand179-189115
α-helix190-1923
β-strand199-20466
α-helix205-2073
β-strand209-21466
Chain L: 6 helices, 25 β-strands
ElementResiduesLengthSheet
β-strand4-747
β-strand10-1348
β-strand19-2577
β-strand3019
β-strand3619
β-strand38-4368
β-strand49-5468
β-strand58-5928
α-helix601
β-strand67-7267
β-strand75-8067
α-helix85-873
β-strand89-9578
α-helix1011
β-strand102-10328
β-strand107-11158
β-strand117110
β-strand120-124511
α-helix125-1273
α-helix128-1325
β-strand135-1451111
β-strand146110
β-strand150-156712
β-strand159-161312
β-strand165-170611
β-strand173113
β-strand176113
β-strand179-1881011
α-helix189-1924
β-strand197-204812
β-strand211-216612

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Heavy Chain Fab fragment of antibody LEM-2/15Hprotein218Mus musculus
Light Chain Fab fragment of antibody LEM-2/15Lprotein218Mus musculus
Matrix metalloproteinase-14Mprotein13Homo sapiensP50281 (AlphaFold model)
Sequence of entity 1 (H), FASTA
>4P3C_1 Heavy Chain Fab fragment of antibody LEM-2/15 (chains H)
EVKLVESGGGLVKPGGSLKLSCAASGFIFSNYAMSWVRQTPEKRLEWVATISGGGRNIYS
LDSVKGRFTFFRDNARNTLYLQMSSLRSEDTAMYFCSRENYGSSFTYWGQGTLVTVSSAK
TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPR
Sequence of entity 2 (L), FASTA
>4P3C_2 Light Chain Fab fragment of antibody LEM-2/15 (chains L)
DVLMTQTPLSLPVGLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPKLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHAPYTFGGGTKLEIKRAADAAPT
VSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYS
MSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN
Sequence of entity 3 (M), FASTA
>4P3C_3 Matrix metalloproteinase-14 (chains M)
FDSAEPWTVRNED

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Water and common crystallization additives (ACT, EDO, EPE, CL) are not listed.

Primary citation

Inhibition mechanism of membrane metalloprotease by an exosite-swiveling conformational antibody. Udi, Y., Grossman, M., Solomonov, I. et al. Structure (2015) 23:104-115. DOI 10.1016/j.str.2014.10.012 · PubMed

Other PDB entries of the same protein (UniProt P50281 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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