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1JIW

Crystal structure of the APR-APRin complex

Functional Information from GO Data
ChainGOidnamespacecontents
I0004866molecular_functionendopeptidase inhibitor activity
I0008191molecular_functionmetalloendopeptidase inhibitor activity
I0010951biological_processnegative regulation of endopeptidase activity
P0001869biological_processnegative regulation of complement activation, lectin pathway
P0004222molecular_functionmetalloendopeptidase activity
P0005509molecular_functioncalcium ion binding
P0005576cellular_componentextracellular region
P0005615cellular_componentextracellular space
P0006508biological_processproteolysis
P0008233molecular_functionpeptidase activity
P0008237molecular_functionmetallopeptidase activity
P0008270molecular_functionzinc ion binding
P0010765biological_processpositive regulation of sodium ion transport
P0045959biological_processnegative regulation of complement activation, classical pathway
P0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN P 481
ChainResidue
ISER1
PHIS176
PHIS180
PHIS186

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 482
ChainResidue
PASP290
PARG253
PGLY255
PTHR257
PASP285
PGLY287

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 483
ChainResidue
PGLY288
PASP290
PTHR327
PGLU329
PHOH491
PHOH520

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 484
ChainResidue
PGLY334
PGLY336
PASP338
PGLY351
PALA353
PASP356

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 485
ChainResidue
PGLY352
PGLY354
PASP356
PGLY369
PALA371
PASP374

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 486
ChainResidue
PGLY370
PGLY372
PASP374
PASP400
PHOH492
PHOH533

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 487
ChainResidue
PASN343
PVAL345
PASN347
PGLY360
PLEU362
PASP365

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 488
ChainResidue
PGLY361
PGLY363
PASP365
PGLU383
PASP390
PHOH495

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA P 489
ChainResidue
PASP446
PSER448
PASP450
PHIS452
PASP454

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLTHEIGHTL
ChainResidueDetails
PTHR173-LEU182

site_idPS00330
Number of Residues19
DetailsHEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DiLygglGaDqLwGGagaD
ChainResidueDetails
PASP356-ASP374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
PGLU177

site_idSWS_FT_FI2
Number of Residues41
DetailsBINDING:
ChainResidueDetails
PHIS176
PASP290
PTHR327
PGLU329
PGLY334
PGLY336
PASP338
PASN343
PVAL345
PASN347
PGLY351
PHIS180
PGLY352
PALA353
PGLY354
PASP356
PGLY360
PGLY361
PLEU362
PGLY363
PASP365
PGLY369
PHIS186
PGLY370
PALA371
PGLY372
PASP374
PGLU383
PASP390
PASP400
PASP446
PSER448
PASP450
PARG253
PHIS452
PASP454
PGLY255
PTHR257
PASP285
PGLY287
PGLY288

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
PGLU177
PGLU194

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
PGLU177

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PDB entries from 2024-07-24

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