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3ZHA

Molecular basis for the action of the collagen-specific chaperone Hsp47 SERPINH1 and its structure-specific client recognition.

Replaces:  4AWR
Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005518molecular_functioncollagen binding
A0005615cellular_componentextracellular space
A0005788cellular_componentendoplasmic reticulum lumen
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005518molecular_functioncollagen binding
B0005615cellular_componentextracellular space
B0005788cellular_componentendoplasmic reticulum lumen
C0004867molecular_functionserine-type endopeptidase inhibitor activity
C0005518molecular_functioncollagen binding
C0005615cellular_componentextracellular space
C0005788cellular_componentendoplasmic reticulum lumen
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005518molecular_functioncollagen binding
D0005615cellular_componentextracellular space
D0005788cellular_componentendoplasmic reticulum lumen
K0004867molecular_functionserine-type endopeptidase inhibitor activity
K0005518molecular_functioncollagen binding
K0005615cellular_componentextracellular space
K0005788cellular_componentendoplasmic reticulum lumen
L0004867molecular_functionserine-type endopeptidase inhibitor activity
L0005518molecular_functioncollagen binding
L0005615cellular_componentextracellular space
L0005788cellular_componentendoplasmic reticulum lumen
P0004867molecular_functionserine-type endopeptidase inhibitor activity
P0005518molecular_functioncollagen binding
P0005615cellular_componentextracellular space
P0005788cellular_componentendoplasmic reticulum lumen
Q0004867molecular_functionserine-type endopeptidase inhibitor activity
Q0005518molecular_functioncollagen binding
Q0005615cellular_componentextracellular space
Q0005788cellular_componentendoplasmic reticulum lumen
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SIN A 1421
ChainResidue
AALA63
AGLU65
AASN66
AVAL313
ATHR314
AHIS315

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SIN C 1418
ChainResidue
CASN66
CTHR314
CHIS315
CALA63
CVAL64
CGLU65

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SIN K 1415
ChainResidue
KALA63
KGLU65
KASN66
KTHR314
KHIS315
KHOH2002

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SIN P 1416
ChainResidue
PALA63
PGLU65
PASN66
PTHR314
PHIS315

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SIN Q 1412
ChainResidue
QALA63
QGLU65
QASN66
QVAL313
QTHR314
QHIS315
QHOH2002

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FYADHPFIFlV
ChainResidueDetails
APHE382-VAL392

246031

PDB entries from 2025-12-10

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