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5HQ1

Comment on S. W. M. Tanley and J. R. Helliwell Structural dynamics of cisplatin binding to histidine in a protein Struct. Dyn. 1, 034701 (2014) regarding the refinement of 4mwk, 4mwm, 4mwn and 4oxe and the method we have adopted.

Replaces:  4MWM
Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue DMS A 201
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108

site_idAC2
Number of Residues7
Detailsbinding site for residue CL A 202
ChainResidue
ATHR69
ASER72
AHOH335
AHOH357
AASN65
AGLY67
AARG68

site_idAC3
Number of Residues7
Detailsbinding site for residue NO3 A 203
ChainResidue
AARG21
AASN65
AASP66
APRO79
ACYS80
ASER81
AHOH312

site_idAC4
Number of Residues7
Detailsbinding site for residue NO3 A 204
ChainResidue
AASN46
ATHR47
AASP48
ALYS97
AHOH308
AHOH339
AHOH354

site_idAC5
Number of Residues4
Detailsbinding site for residue PT A 205
ChainResidue
AHIS15
ATHR89
APT206
APT207

site_idAC6
Number of Residues3
Detailsbinding site for residue PT A 206
ChainResidue
AHIS15
APT205
APT207

site_idAC7
Number of Residues3
Detailsbinding site for residue PT A 207
ChainResidue
AHIS15
APT205
APT206

site_idAC8
Number of Residues3
Detailsbinding site for residue PT A 208
ChainResidue
AHIS15
ACL209
ACL212

site_idAC9
Number of Residues2
Detailsbinding site for residue CL A 209
ChainResidue
APT208
ACL212

site_idAD1
Number of Residues8
Detailsbinding site for residue NO3 A 210
ChainResidue
ASER24
ALEU25
AGLY26
AGLN41
AGLN121
AILE124
AHOH363
AHOH372

site_idAD2
Number of Residues7
Detailsbinding site for residue NO3 A 211
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79
AARG112
ALYS116

site_idAD3
Number of Residues5
Detailsbinding site for residue CL A 212
ChainResidue
AHIS15
AASN93
ALYS96
APT208
ACL209

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
ACYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASP101

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
AGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASN46
AASP48
ASER50
AASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
AASN59

226707

PDB entries from 2024-10-30

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