4ILW: Metalloproteinase inhibitor 2

Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-2 (TIMP-2). Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Nov 2013.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,564
Mol. weight: 81.21 kDa
Ligands: ZN, CA
Released: 13 Nov 2013

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

Secondary structure: helices and β-sheets

4ILW contains 24 α-helices and 37 β-strands across 4 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: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	1
α-helix	8-14	7
β-strand	17-32	16	2
α-helix	38-39	2
β-strand	40-54	15	2
α-helix	59-60	2
β-strand	62-65	4	2
α-helix	69-71	3
β-strand	83-90	8	2
β-strand	95-97	3	2
β-strand	104-106	3	2
α-helix	107-109	3
α-helix	112-117	6
α-helix	121-124	4
β-strand	129-132	4	3
β-strand	145-148	4	3
α-helix	150-154	5
α-helix	160-164	5
β-strand	166-169	4	4
β-strand	175-178	4	4

Chain B: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	5
α-helix	8-14	7
β-strand	17-30	14	6
α-helix	38-40	3
β-strand	41-54	14	6
α-helix	59-60	2
β-strand	62-65	4	6
α-helix	69-71	3
β-strand	83-90	8	6
β-strand	95-97	3	6
β-strand	104-106	3	6
α-helix	107-109	3
α-helix	112-117	6
α-helix	121-124	4
β-strand	129-132	4	7
β-strand	145-148	4	7
α-helix	150-154	5
α-helix	160-164	5
β-strand	165-169	5	8
β-strand	175-179	5	8

Chain D: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	112-117	6	1
α-helix	126-141	16
β-strand	147-150	4	1
β-strand	158-163	6	1
β-strand	179-183	5	1
β-strand	194-197	4	1
β-strand	202-203	2	9
β-strand	209-210	2	9
α-helix	211-222	12
α-helix	252-262	11

Chain F: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	112-117	6	5
α-helix	126-141	16
β-strand	147-150	4	5
β-strand	158-163	6	5
β-strand	179-183	5	5
β-strand	194-197	4	5
β-strand	202-203	2	10
β-strand	209-210	2	10
α-helix	211-222	12
β-strand	238	1	5
α-helix	252-262	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metalloproteinase inhibitor 2	A, B	protein	194	Homo sapiens	P16035 (AlphaFold model)
Stromelysin-2	D, F	protein	165	Homo sapiens	P09238 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4ILW_1 Metalloproteinase inhibitor 2 (chains A, B)
CSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDI
EFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNH
RYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRG
AAPPKQEFLDIEDP

Sequence of entity 2 (D, F), FASTA

>4ILW_2 Stromelysin-2 (chains D, F)
FSSFPGMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADI
MISFAVKEHGDFYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHE
LGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4
CA	Calcium ion	Ca	6

Primary citation

Matrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP Complexes. Batra, J., Soares, A.S., Mehner, C. et al. PLoS One (2013) 8:e75836-e75836. DOI 10.1371/journal.pone.0075836 · PubMed

Other PDB entries of the same protein (UniProt P16035 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1BR9 2.1 Å, Human tissue inhibitor of metalloproteinase-2
1GXD 3.1 Å, proMMP-2/TIMP-2 complex
2TMP N-terminal domain of tissue inhibitor of metalloproteinase-2 (N-timp-2), NMR, 49…

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