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3LJT

Crystal Structure of the Catalytic Domain of ADAMTS-5 in Complex with an Amino-2-indanol compound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE LA3 A 801
ChainResidue
AASP377
AHIS420
ALEU438
ASER440
ASER441
ALEU443
AILE446
AZN901
AHOH5040
AHOH5296
ATHR378
ALEU379
AGLY380
APHE406
ATHR407
AHIS410
AGLU411
AHIS414

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 802
ChainResidue
AGLY372
AGLY385
ATHR386
ASER389
AHIS468
AHOH5006
AHOH5217

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
AHIS410
AHIS414
AHIS420
ALA3801

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 902
ChainResidue
AGLU270
AASP360
ACYS471
AASP474
AHOH5009
AHOH5031

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 903
ChainResidue
AGLU270
AASP474
ALEU475
AHOH5068
AHOH5103
AHOH5157

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 904
ChainResidue
AASP369
ALEU370
ACYS376
ATHR378
AGLU398
AHOH5014

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVAHEIGHLL
ChainResidueDetails
ATHR407-LEU416

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:18042673
ChainResidueDetails
AGLU411

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18042673
ChainResidueDetails
AHIS410
AHIS414
AHIS420

218853

PDB entries from 2024-04-24

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