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2V4B

Crystal Structure of Human ADAMTS-1 catalytic Domain and Cysteine- Rich Domain (apo-form)

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 A1552
ChainResidue
AHIS401
AHIS405
AHIS411
AHOH2133

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B1553
ChainResidue
BHIS401
BHIS405
BHIS411

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A1553
ChainResidue
AASP465
AHOH2044
AHOH2091
AGLU261
AASP344

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A1554
ChainResidue
AGLU315
AGLU320
AHOH2027

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A1555
ChainResidue
AGLU494
AHOH2106
BHIS313
BHOH2003
BHOH2007

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A1556
ChainResidue
AHIS280
AHOH2013
BASP483
BHOH2057

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI A1557
ChainResidue
AGLU261
AASP344
AASP351
ACYS462
AASP465
AHOH2089

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD B1554
ChainResidue
AASP483
BHIS280
BHOH2010

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI B1555
ChainResidue
AHIS313
AHOH2012
BGLU494
BASP495

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD B1556
ChainResidue
BGLU261
BASP344
BASP465
BHOH2024

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI B1557
ChainResidue
BGLU261
BASP344
BASP351
BCYS462
BASP465
BHOH2046

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A1558
ChainResidue
AHIS313
AHOH2006
AHOH2009
AHOH2024
BGLU494

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A1559
ChainResidue
AGLU320
AHOH2027

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A1560
ChainResidue
ALYS308
AHIS339

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A1561
ChainResidue
AHIS428
AHOH2075

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI A1562
ChainResidue
AGLU494
AASP495
BHIS313

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A1563
ChainResidue
AHIS498
AHOH2109

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A1564
ChainResidue
AHIS525
BLEU519

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B1558
ChainResidue
BHIS439
BASP530
BASN542
BHOH2071

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI B1559
ChainResidue
BHIS428
BHOH2036

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI B1560
ChainResidue
BHIS459
BHOH2045

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI B1561
ChainResidue
BHIS498
BHOH2064

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A1565
ChainResidue
AHIS439
AASP530
AASN542
AHOH2126

site_idCC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A1566
ChainResidue
AASP360
ALEU361
ACYS367
ATHR369
AGLU389
AHOH2049

site_idCC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B1562
ChainResidue
BASP360
BLEU361
BCYS367
BTHR369
BGLU389
BNA1563

site_idCC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A1567
ChainResidue
AASP360
ACYS367
AHOH2049

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B1563
ChainResidue
BASP360
BCYS367
BNA1562

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGeDSKHCPD
ChainResidueDetails
APHE492-ASP501

site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TTAHELGHVF
ChainResidueDetails
ATHR398-PHE407

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:17897672
ChainResidueDetails
AGLU402
BGLU402

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:17897672
ChainResidueDetails
AGLU261
BASP344
BASP351
BHIS401
BHIS405
BHIS411
BCYS462
BASP465
AASP344
AASP351
AHIS401
AHIS405
AHIS411
ACYS462
AASP465
BGLU261

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN547
BASN547

237735

PDB entries from 2025-06-18

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