7AUW

Inhibitory complex of human meprin beta with mouse fetuin-B.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016020	cellular_component	membrane
B	0004869	molecular_function	cysteine-type endopeptidase inhibitor activity
B	0005615	cellular_component	extracellular space
C	0004222	molecular_function	metalloendopeptidase activity
C	0006508	biological_process	proteolysis
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0016020	cellular_component	membrane
D	0004869	molecular_function	cysteine-type endopeptidase inhibitor activity
D	0005615	cellular_component	extracellular space

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVQHEFLHAL

Chain	Residue	Details
A	THR149-LEU158

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site_id	PS00740
Number of Residues	41
Details	MAM_1 MAM domain signature. GfFMhfdSssvnvgatav.LesrtLypkrgfqCLqFyLynsG

Chain	Residue	Details
A	GLY309-GLY349

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site_id	PS01254
Number of Residues	119
Details	FETUIN_1 Fetuin family signature 1. CNDsevlavagfalqninrdqkdgymlslnrvhdvrehyqedmgslfyltldvletdCHvlsrkaqkdCkprmfyesvygq..CkamfhinkprrvlylpaynCtlrpvskrkthttCpdC

Chain	Residue	Details
B	CYS39-CYS157

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site_id	PS01255
Number of Residues	10
Details	FETUIN_2 Fetuin family signature 2. DvLETdCHvL

Chain	Residue	Details
B	ASP90-LEU99

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9UGM5

Chain	Residue	Details
D	SER321
B	SER321

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
C	HIS156
C	HIS162
D	ASN40
A	HIS162
C	HIS152
B	ASN40

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17330941

Chain	Residue	Details
B	ASN139
D	ASN139

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site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000250|UniProtKB:Q58D62

Chain	Residue	Details
B	THR292
B	THR295
D	THR292
D	THR295
A	ASN445
A	ASN547
A	ASN592
C	ASN218
C	ASN254
C	ASN370
C	ASN436
C	ASN445
C	ASN547
C	ASN592

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site_id	SWS_FT_FI5
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN421
C	ASN421

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site_id	SWS_FT_FI6
Number of Residues	4
Details	CARBOHYD: O-linked (GalNAc...) serine => ECO:0000255

Chain	Residue	Details
A	SER593
A	SER603
C	SER593
C	SER603

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site_id	SWS_FT_FI7
Number of Residues	4
Details	CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000255

Chain	Residue	Details
A	THR594
A	THR599
C	THR594
C	THR599

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