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4FVL

Human collagenase 3 (MMP-13) full form with peptides from pro-domain

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B
(A, B)
Collagenase 3polymer36842284.62UniProt (P45452)
Pfam (PF00413)
Pfam (PF00045)
Homo sapiens (human)Matrix metalloproteinase-13, MMP-13
2C, D
(C, D)
Collagenase 3, pro-domain peptidepolymer202520.72UniProt (P45452)
Pfam (PF01471)
Homo sapiens (human)Matrix metalloproteinase-13, MMP-13
3E, F, KA, LA
(A, B)
ZINC IONnon-polymer65.44Chemie (ZN)
4G, H, I, J, K...
(A, B)
CALCIUM IONnon-polymer40.110Chemie (CA)
5L, M, RA
(A, B)
CHLORIDE IONnon-polymer35.53Chemie (CL)
6N, O, P, SA, TA...
(A, B)
GLYCEROLnon-polymer92.110Chemie (GOL)
7AA, AB, BA, BB, CA...
(A, B, C)
S-1,2-PROPANEDIOLnon-polymer76.128Chemie (PGO)
8FA, GA, HA, IA, JA...
(A, B, D)
DI(HYDROXYETHYL)ETHERnon-polymer106.19Chemie (PEG)
9QB, RB, SB, TB
(A, B, C, D)
waterwater18.0234Chemie (HOH)
Sequence modifications
A, B: 104 - 471 (UniProt: P45452)
PDBExternal DatabaseDetails
Ala 223Glu 223engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains4
Total formula weight89610.7
Non-Polymers*Number of molecules64
Total formula weight4775.4
All*Total formula weight94386.1
*Water molecules are not included.

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PDB entries from 2024-10-30

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