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3HB2

PrtC methionine mutants: M226I

Functional Information from GO Data
ChainGOidnamespacecontents
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
P0016787molecular_functionhydrolase activity
P0030198biological_processextracellular matrix organization
P0030574biological_processcollagen catabolic process
P0031012cellular_componentextracellular matrix
P0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 480
ChainResidue
PARG265
PGLY267
PSER269
PASP297
PGLY299
PASP302

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 481
ChainResidue
PGLU341
PHOH532
PHOH533
PGLY300
PASP302
PTHR339

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 482
ChainResidue
PGLY346
PGLY348
PASP350
PGLY363
PALA365
PASP368

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 483
ChainResidue
PASN355
PALA357
PASN359
PGLY372
PALA374
PASP377

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 484
ChainResidue
PGLY364
PGLY366
PASP368
PGLY381
PALA383
PASP386

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 485
ChainResidue
PHOH17
PGLY382
PGLY384
PASP386
PGLN408
PASP412

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN P 486
ChainResidue
PHIS188
PHIS192
PHIS198
PHOH556

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 487
ChainResidue
PGLY373
PGLY375
PASP377
PASP395
PASP402
PHOH535

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL P 1
ChainResidue
PASN355
PSER356
PALA374
PHOH895
PHOH981

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL P 3
ChainResidue
PTYR146
PARG467
PHOH758

Functional Information from PROSITE/UniProt
site_idPS00330
Number of Residues19
DetailsHEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DvLyggaGaDtLyGGagrD
ChainResidueDetails
PASP368-ASP386

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
PALA189

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
PHIS188
PHIS192
PTYR228

site_idSWS_FT_FI3
Number of Residues31
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
PARG265
PGLY348
PASP350
PASN355
PALA357
PASN359
PGLY363
PGLY364
PALA365
PGLY366
PASP368
PGLY267
PGLY372
PGLY373
PGLY375
PASP377
PGLY381
PGLY382
PALA383
PGLY384
PASP386
PASP395
PASP297
PASP402
PASP412
PGLY299
PGLY300
PASP302
PTHR339
PGLU341
PGLY346

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PDB entries from 2024-04-24

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