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3HDA

PrtC methionine mutants: M226A_DESY

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
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
PHOH634
PHOH635
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
PHOH10
PGLY382
PGLY384
PASP386
PGLN408
PASP412

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA P 487
ChainResidue
PGLY373
PGLY375
PASP377
PASP395
PASP402
PHOH636

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL P 1
ChainResidue
PARG265
PGLY267
PSER269
PHOH659

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL P 3
ChainResidue
PGLN110
PSER113
PHOH508
PHOH694

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TFTHEIGHAL
ChainResidueDetails
PTHR185-LEU194

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 Residues17
DetailsRepeat: {"description":"Hemolysin-type calcium-binding 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues17
DetailsRepeat: {"description":"Hemolysin-type calcium-binding 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues17
DetailsRepeat: {"description":"Hemolysin-type calcium-binding 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues31
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qib
ChainResidueDetails
PGLU189

239803

PDB entries from 2025-08-06

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