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6YJM

Crystal Structure of the Catalytic Domain of ADAMTS-5 in Complex with the Inhibitor GLPG1972

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 501
ChainResidue
AHIS410
AHIS414
AHIS420
AOU5505

site_idAC2
Number of Residues7
Detailsbinding site for residue CA A 502
ChainResidue
ACA503
AHOH608
AGLU270
AASP353
AASP360
ACYS471
AASP474

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 503
ChainResidue
AGLU270
AASP353
AASP474
ACA502
AHOH610
AHOH612

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 504
ChainResidue
AASP369
ALEU370
ACYS376
ATHR378
AGLU398
AHOH639

site_idAC5
Number of Residues19
Detailsbinding site for residue OU5 A 505
ChainResidue
ATHR378
ALEU379
AGLY380
AMET381
AHIS403
APHE406
ATHR407
AHIS410
AGLU411
AHIS414
AHIS420
AARG437
ALEU438
ASER440
ASER441
ATHR444
AILE446
AZN501
AHOH619

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BHIS410
BHIS414
BHIS420
BOU5505

site_idAC7
Number of Residues7
Detailsbinding site for residue CA B 502
ChainResidue
BGLU270
BASP353
BASP360
BCYS471
BASP474
BCA503
BHOH605

site_idAC8
Number of Residues6
Detailsbinding site for residue CA B 503
ChainResidue
BGLU270
BASP353
BASP474
BCA502
BHOH607
BHOH614

site_idAC9
Number of Residues6
Detailsbinding site for residue CA B 504
ChainResidue
BASP369
BLEU370
BCYS376
BTHR378
BGLU398
BHOH630

site_idAD1
Number of Residues18
Detailsbinding site for residue OU5 B 505
ChainResidue
BTHR378
BLEU379
BGLY380
BHIS403
BPHE406
BHIS410
BGLU411
BHIS420
BARG437
BLEU438
BSER440
BSER441
BLEU443
BTHR444
BILE446
BZN501
BHOH603
BHOH623

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 Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:18042673
ChainResidueDetails
AGLU411
BGLU411

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18042673
ChainResidueDetails
AHIS410
AHIS414
AHIS420
BHIS410
BHIS414
BHIS420

224004

PDB entries from 2024-08-21

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