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4KXI

Crystallographic study of the complex of Ni(II) Schiff base complex and HEW Lysozyme

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 Residues4
DetailsBINDING SITE FOR RESIDUE NI A 201
ChainResidue
ALYS13
ALEU129
ALEU129
ALCP204

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SNF A 202
ChainResidue
AGLN57
AASN59
ATRP108
AHOH354
AHOH356
AHOH357
AHOH359
AHOH360
AGLU35
AASN44
AASN46
AASP52
ALEU56

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LCP A 203
ChainResidue
ASER24
ALEU25
AGLY26
AASN27
AVAL120
AGLN121
AILE124

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LCP A 204
ChainResidue
ALYS13
AARG61
APRO70
APRO70
ALEU129
ANI201

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LCP A 205
ChainResidue
AASP101

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LCP A 206
ChainResidue
AARG5
ALYS33
APHE38
ATRP123

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LCP A 207
ChainResidue
APHE34
AARG114
ALYS116
AGLY117
ATHR118
AHOH311
AHOH325
AHOH336
AHOH355

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 208
ChainResidue
AGLY71
AGLY71

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

227344

PDB entries from 2024-11-13

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