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4GER

Crystal structure of Gentlyase, the neutral metalloprotease of Paenibacillus polymyxa

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS135
AHIS139
AGLU159
AHOH501

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AHOH503
AHOH607
AASP129
AASP131
AGLN170
AASP178
AASP179

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP53
AASP55
AVAL57
AHOH557
AHOH565
AHOH573

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ATYR181
ATHR182
AILE185
AASP188
AHOH556
AHOH683

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE THR A 405
ChainResidue
AASN105
AALA106
AGLU136
AARG191
AHIS219
ALYS406
AHOH501

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LYS A 406
ChainResidue
AASN104
AASN105
APHE123
AHIS219
ATHR405

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BHIS135
BHIS139
BGLU159
BHOH501

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BASP129
BASP131
BGLN170
BASP178
BASP179
BHOH512
BHOH625

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BASP53
BASP55
BVAL57
BHOH595
BHOH633
BHOH643

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BTYR181
BTHR182
BILE185
BASP188
BHOH624
BHOH631

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE THR B 405
ChainResidue
BASN105
BALA106
BPHE126
BGLU136
BARG191
BHIS219
BLYS406

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LYS B 406
ChainResidue
BASN104
BASN105
BPHE123
BHIS219
BTHR405

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVGHELTHGV
ChainResidueDetails
AVAL132-VAL141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-12-17

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