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1K7G

PrtC from Erwinia chrysanthemi

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0031012cellular_componentextracellular matrix
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 480
ChainResidue
AARG265
AGLY267
ASER269
AASP297
AGLY299
AASP302

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 481
ChainResidue
AGLU341
AHOH998
AHOH999
AGLY300
AASP302
ATHR339

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 482
ChainResidue
AGLY346
AGLY348
AASP350
AGLY363
AALA365
AASP368

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 483
ChainResidue
AASN355
AALA357
AASN359
AGLY372
AALA374
AASP377

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 484
ChainResidue
AGLY364
AGLY366
AASP368
AGLY381
AALA383
AASP386

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 485
ChainResidue
AGLY382
AGLY384
AASP386
AGLN408
AASP412
AHOH518

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 486
ChainResidue
AHIS188
AHIS192
AHIS198
APO4488

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 487
ChainResidue
AGLY373
AGLY375
AASP377
AASP395
AASP402
AHOH547

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 488
ChainResidue
AALA150
ATYR151
AHIS188
AGLU189
AHIS192
AHIS198
ATYR228
AZN486
AHOH600

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TFTHEIGHAL
ChainResidueDetails
ATHR185-LEU194

site_idPS00330
Number of Residues19
DetailsHEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DvLyggaGaDtLyGGagrD
ChainResidueDetails
AASP368-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 Residues3
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 Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AMET226
AGLU189

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU189

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU189
AGLU206

246905

PDB entries from 2025-12-31

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