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1M21

Crystal structure analysis of the peptide amidase PAM in complex with the competitive inhibitor chymostatin

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR CHAIN C OF CHYMOSTATIN
ChainResidue
AALA171
ACYS229
AILE254
AARG360
ALEU363
ALEU407
APHE468
ATYR473
AHOH902
AHOH933
AASN172
APHE173
ASER180
ACYS200
AGLY201
ASER202
AASP224
ASER226

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR CHAIN D OF CHYMOSTATIN
ChainResidue
BALA171
BASN172
BPHE173
BSER180
BCYS200
BGLY201
BSER202
BASP224
BSER226
BCYS229
BILE254
BARG360
BLEU363
BLEU407
BPHE468
BTYR473
BHOH1937

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 12367528
ChainResidueDetails
ASER226
ALYS123
ASER202

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 12367528
ChainResidueDetails
BSER226
BLYS123
BSER202

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PDB entries from 2024-07-10

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